Madden DR


Full name : Madden Dean R

First name : Dean R

Mail : Department of Biochemistry , Geisel School of Medicine at Dartmouth, Hanover, New Hampshire 03755

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Country : USA

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References (14)

Title : Molecular basis for the transcriptional regulation of an epoxide-based virulence circuit in Pseudomonas aeruginosa - He_2024_bioRxiv__
Author(s) : He S , Taher NM , Hvorecny KL , Ragusa MJ , Bahl CD , Hickman AB , Dyda F , Madden DR
Ref : Biorxiv , : , 2024
Abstract : The opportunistic pathogen Pseudomonas aeruginosa infects cystic fibrosis (CF) patient airways and produces a virulence factor Cif that is associated with worse outcomes. Cif is an epoxide hydrolase that reduces cell-surface abundance of the cystic fibrosis transmembrane conductance regulator (CFTR) and sabotages pro-resolving signals. Its expression is regulated by a divergently transcribed TetR family transcriptional repressor. CifR represents the first reported epoxide-sensing bacterial transcriptional regulator, but neither its interaction with cognate operator sequences nor the mechanism of activation has been investigated. Using biochemical and structural approaches, we uncovered the molecular mechanisms controlling this complex virulence operon. We present here the first molecular structures of CifR alone and in complex with operator DNA, resolved in a single crystal lattice. Significant conformational changes between these two structures suggest how CifR regulates the expression of the virulence gene cif . Interactions between the N-terminal extension of CifR with the DNA minor groove of the operator play a significant role in the operator recognition of CifR. We also determined that cysteine residue Cys107 is critical for epoxide sensing and DNA release. These results offer new insights into the stereochemical regulation of an epoxide-based virulence circuit in a critically important clinical pathogen.
ESTHER : He_2024_bioRxiv__
PubMedSearch : He_2024_bioRxiv__
PubMedID: 38293063
Gene_locus related to this paper: pseae-PA2934

Title : Biochemical and Structural Characterization of Two Cif-Like Epoxide Hydrolases from Burkholderia cenocepacia - Taher_2021_Curr.Res.Struct.Biol_3_72
Author(s) : Taher NM , Hvorecny KL , Burke CM , Gilman MSA , Heussler GE , Adolf-Bryfogle J , Bahl CD , O'Tool GA , Madden DR
Ref : Current Research in Structural Biology , 3 :72 , 2021
Abstract : Epoxide hydrolases catalyze the conversion of epoxides to vicinal diols in a range of cellular processes such as signaling, detoxification, and virulence. These enzymes typically utilize a pair of tyrosine residues to orient the substrate epoxide ring in the active site and stabilize the hydrolysis intermediate. A new subclass of epoxide hydrolases that utilize a histidine in place of one of the tyrosines was established with the discovery of the CFTR Inhibitory Factor (Cif) from Pseudomonas aeruginosa. Although the presence of such Cif-like epoxide hydrolases was predicted in other opportunistic pathogens based on sequence analyses, only Cif and its homologue aCif from Acinetobacter nosocomialis have been characterized. Here we report the biochemical and structural characteristics of Cfl1 and Cfl2, two Cif-like epoxide hydrolases from Burkholderia cenocepacia. Cfl1 is able to hydrolyze xenobiotic as well as biological epoxides that might be encountered in the environment or during infection. In contrast, Cfl2 shows very low activity against a diverse set of epoxides. The crystal structures of the two proteins reveal quaternary structures that build on the well-known dimeric assembly of the alpha/beta hydrolase domain, but broaden our understanding of the structural diversity encoded in novel oligomer interfaces. Analysis of the interfaces reveals both similarities and key differences in sequence conservation between the two assemblies, and between the canonical dimer and the novel oligomer interfaces of each assembly. Finally, we discuss the effects of these higher-order assemblies on the intra-monomer flexibility of Cfl1 and Cfl2 and their possible roles in regulating enzymatic activity.
ESTHER : Taher_2021_Curr.Res.Struct.Biol_3_72
PubMedSearch : Taher_2021_Curr.Res.Struct.Biol_3_72
PubMedID: 34235487
Gene_locus related to this paper: burch-a0az59 , burch-a0b0f8

Title : Pseudomonas aeruginosa sabotages the generation of host proresolving lipid mediators - Flitter_2017_Proc.Natl.Acad.Sci.U.S.A_114_136
Author(s) : Flitter BA , Hvorecny KL , Ono E , Eddens T , Yang J , Kwak DH , Bahl CD , Hampton TH , Morisseau C , Hammock BD , Liu X , Lee JS , Kolls JK , Levy BD , Madden DR , Bomberger JM
Ref : Proc Natl Acad Sci U S A , 114 :136 , 2017
Abstract : Recurrent Pseudomonas aeruginosa infections coupled with robust, damaging neutrophilic inflammation characterize the chronic lung disease cystic fibrosis (CF). The proresolving lipid mediator, 15-epi lipoxin A4 (15-epi LXA4), plays a critical role in limiting neutrophil activation and tissue inflammation, thus promoting the return to tissue homeostasis. Here, we show that a secreted P. aeruginosa epoxide hydrolase, cystic fibrosis transmembrane conductance regulator inhibitory factor (Cif), can disrupt 15-epi LXA4 transcellular biosynthesis and function. In the airway, 15-epi LXA4 production is stimulated by the epithelial-derived eicosanoid 14,15-epoxyeicosatrienoic acid (14,15-EET). Cif sabotages the production of 15-epi LXA4 by rapidly hydrolyzing 14,15-EET into its cognate diol, eliminating a proresolving signal that potently suppresses IL-8-driven neutrophil transepithelial migration in vitro. Retrospective analyses of samples from patients with CF supported the translational relevance of these preclinical findings. Elevated levels of Cif in bronchoalveolar lavage fluid were correlated with lower levels of 15-epi LXA4, increased IL-8 concentrations, and impaired lung function. Together, these findings provide structural, biochemical, and immunological evidence that the bacterial epoxide hydrolase Cif disrupts resolution pathways during bacterial lung infections. The data also suggest that Cif contributes to sustained pulmonary inflammation and associated loss of lung function in patients with CF.
ESTHER : Flitter_2017_Proc.Natl.Acad.Sci.U.S.A_114_136
PubMedSearch : Flitter_2017_Proc.Natl.Acad.Sci.U.S.A_114_136
PubMedID: 27980032
Gene_locus related to this paper: pseae-PA2934

Title : The cif Virulence Factor Gene Is Present in Isolates From Patients With Pseudomonas aeruginosa Keratitis - Bahl_2017_Cornea_36_358
Author(s) : Bahl CD , St Laurent JD , Karthikeyan RS , Priya JL , Prajna L , Zegans ME , Madden DR
Ref : Cornea , 36 :358 , 2017
Abstract : PURPOSE: To determine whether the cif gene is present in pathogenic Pseudomonas aeruginosa isolates from patients with bacterial keratitis at Aravind Eye Hospital, a referral eye care center in southern India, and from corresponding environmental isolates.
METHODS: Polymerase chain reaction amplification was performed on strains of P. aeruginosa isolated from ocular infections and environmental soil samples were collected from the area surrounding Aravind Eye Hospital. DNA sequencing of 16S ribosomal DNA amplicons was performed to verify strain identity.
RESULTS: We determined that 45 of 48 patient isolates carry a genomic copy of cif. Analysis of a catalog of environmental strains previously isolated from the surrounding area revealed that only 4 of 10 P. aeruginosa strains and 1 of 14 strains of related species carry the cif gene.
CONCLUSIONS: This is the first study to show that P. aeruginosa strains with ocular pathogenicity carry the cif gene and that the presence of this gene may be enriched over its prevalence in the environment. Taken together, these results suggest a potential role for Cif in acute bacterial keratitis.
ESTHER : Bahl_2017_Cornea_36_358
PubMedSearch : Bahl_2017_Cornea_36_358
PubMedID: 28079684

Title : Active-Site Flexibility and Substrate Specificity in a Bacterial Virulence Factor: Crystallographic Snapshots of an Epoxide Hydrolase - Hvorecny_2017_Structure_25_697
Author(s) : Hvorecny KL , Bahl CD , Kitamura S , Lee KSS , Hammock BD , Morisseau C , Madden DR
Ref : Structure , 25 :697 , 2017
Abstract : Pseudomonas aeruginosa secretes an epoxide hydrolase with catalytic activity that triggers degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and perturbs other host defense networks. Targets of this CFTR inhibitory factor (Cif) are largely unknown, but include an epoxy-fatty acid. In this class of signaling molecules, chirality can be an important determinant of physiological output and potency. Here we explore the active-site chemistry of this two-step alpha/beta-hydrolase and its implications for an emerging class of virulence enzymes. In combination with hydrolysis data, crystal structures of 15 trapped hydroxyalkyl-enzyme intermediates reveal the stereochemical basis of Cif's substrate specificity, as well as its regioisomeric and enantiomeric preferences. The structures also reveal distinct sets of conformational changes that enable the active site to expand dramatically in two directions, accommodating a surprising array of potential physiological epoxide targets. These new substrates may contribute to Cif's diverse effects in vivo, and thus to the success of P. aeruginosa and other pathogens during infection.
ESTHER : Hvorecny_2017_Structure_25_697
PubMedSearch : Hvorecny_2017_Structure_25_697
PubMedID: 28392259
Gene_locus related to this paper: pseae-PA2934

Title : Visualizing the Mechanism of Epoxide Hydrolysis by the Bacterial Virulence Enzyme Cif - Bahl_2016_Biochemistry_55_788
Author(s) : Bahl CD , Hvorecny KL , Morisseau C , Gerber SA , Madden DR
Ref : Biochemistry , 55 :788 , 2016
Abstract : The CFTR inhibitory factor (Cif) is an epoxide hydrolase (EH) virulence factor secreted by the bacterium Pseudomonas aeruginosa. Sequence alignments reveal a pattern of Cif-like substitutions that proved to be characteristic of a new subfamily of bacterial EHs. At the same time, crystallographic and mutagenetic data suggest that EH activity is required for virulence and that Cif's active site remains generally compatible with a canonical two-step EH mechanism. A hallmark of this mechanism is the formation of a covalent hydroxyalkyl-enzyme intermediate by nucleophilic attack. In several well-studied EHs, this intermediate has been captured at near stoichiometric levels, presumably reflecting rate-limiting hydrolysis. Here we show by mass spectrometry that only minimal levels of the expected intermediate can be trapped with WT Cif. In contrast, substantial amounts of intermediate are recovered from an active-site mutant (Cif-E153Q) that selectively targets the second, hydrolytic release step. Utilizing Cif-E153Q and a previously reported nucleophile mutant (Cif-D129S), we then captured Cif in the substrate-bound, hydroxyalkyl-intermediate, and product-bound states for 1,2-epoxyhexane, yielding the first crystallographic snapshots of an EH at these key stages along the reaction coordinate. Taken together, our data illuminate the proposed two-step hydrolytic mechanism of a new class of bacterial virulence factor. They also suggest that the failure of WT Cif to accumulate a covalent hydroxyalkyl-enzyme intermediate reflects an active-site chemistry in which hydrolysis is no longer the rate-limiting step, a noncanonical kinetic regime that may explain similar observations with a number of other EHs.
ESTHER : Bahl_2016_Biochemistry_55_788
PubMedSearch : Bahl_2016_Biochemistry_55_788
PubMedID: 26752215
Gene_locus related to this paper: pseae-PA2934

Title : Rational Design of Potent and Selective Inhibitors of an Epoxide Hydrolase Virulence Factor from Pseudomonas aeruginosa - Kitamura_2016_J.Med.Chem_59_4790
Author(s) : Kitamura S , Hvorecny KL , Niu J , Hammock BD , Madden DR , Morisseau C
Ref : Journal of Medicinal Chemistry , 59 :4790 , 2016
Abstract : The virulence factor cystic fibrosis transmembrane conductance regulator (CFTR) inhibitory factor (Cif) is secreted by Pseudomonas aeruginosa and is the founding member of a distinct class of epoxide hydrolases (EHs) that triggers the catalysis-dependent degradation of the CFTR. We describe here the development of a series of potent and selective Cif inhibitors by structure-based drug design. Initial screening revealed 1a (KB2115), a thyroid hormone analog, as a lead compound with low micromolar potency. Structural requirements for potency were systematically probed, and interactions between Cif and 1a were characterized by X-ray crystallography. On the basis of these data, new compounds were designed to yield additional hydrogen bonding with residues of the Cif active site. From this effort, three compounds were identified that are 10-fold more potent toward Cif than our first-generation inhibitors and have no detectable thyroid hormone-like activity. These inhibitors will be useful tools to study the pathological role of Cif and have the potential for clinical application.
ESTHER : Kitamura_2016_J.Med.Chem_59_4790
PubMedSearch : Kitamura_2016_J.Med.Chem_59_4790
PubMedID: 27120257
Gene_locus related to this paper: pseae-PA2934

Title : Inhibiting an Epoxide Hydrolase Virulence Factor from Pseudomonas aeruginosa Protects CFTR - Bahl_2015_Angew.Chem.Int.Ed.Engl_54_9881
Author(s) : Bahl CD , Hvorecny KL , Bomberger JM , Stanton BA , Hammock BD , Morisseau C , Madden DR
Ref : Angew Chem Int Ed Engl , 54 :9881 , 2015
Abstract : Opportunistic pathogens exploit diverse strategies to sabotage host defenses. Pseudomonas aeruginosa secretes the CFTR inhibitory factor Cif and thus triggers loss of CFTR, an ion channel required for airway mucociliary defense. However, the mechanism of action of Cif has remained unclear. It catalyzes epoxide hydrolysis, but there is no known role for natural epoxides in CFTR regulation. It was demonstrated that the hydrolase activity of Cif is strictly required for its effects on CFTR. A small-molecule inhibitor that protects this key component of the mucociliary defense system was also uncovered. These results provide a basis for targeting the distinctive virulence chemistry of Cif and suggest an unanticipated role of physiological epoxides in intracellular protein trafficking.
ESTHER : Bahl_2015_Angew.Chem.Int.Ed.Engl_54_9881
PubMedSearch : Bahl_2015_Angew.Chem.Int.Ed.Engl_54_9881
PubMedID: 26136396
Gene_locus related to this paper: pseae-PA2934

Title : Signature motifs identify an acinetobacter cif virulence factor with epoxide hydrolase activity - Bahl_2014_J.Biol.Chem_289_7460
Author(s) : Bahl CD , Hvorecny KL , Bridges AA , Ballok AE , Bomberger JM , Cady KC , O'Toole GA , Madden DR
Ref : Journal of Biological Chemistry , 289 :7460 , 2014
Abstract : Endocytic recycling of the cystic fibrosis transmembrane conductance regulator (CFTR) is blocked by the CFTR inhibitory factor (Cif). Originally discovered in Pseudomonas aeruginosa, Cif is a secreted epoxide hydrolase that is transcriptionally regulated by CifR, an epoxide-sensitive repressor. In this report, we investigate a homologous protein found in strains of the emerging nosocomial pathogens Acinetobacter nosocomialis and Acinetobacter baumannii ("aCif"). Like Cif, aCif is an epoxide hydrolase that carries an N-terminal secretion signal and can be purified from culture supernatants. When applied directly to polarized airway epithelial cells, mature aCif triggers a reduction in CFTR abundance at the apical membrane. Biochemical and crystallographic studies reveal a dimeric assembly with a stereochemically conserved active site, confirming our motif-based identification of candidate Cif-like pathogenic EH sequences. Furthermore, cif expression is transcriptionally repressed by a CifR homolog ("aCifR") and is induced in the presence of epoxides. Overall, this Acinetobacter protein recapitulates the essential attributes of the Pseudomonas Cif system and thus may facilitate airway colonization in nosocomial lung infections.
ESTHER : Bahl_2014_J.Biol.Chem_289_7460
PubMedSearch : Bahl_2014_J.Biol.Chem_289_7460
PubMedID: 24474692
Gene_locus related to this paper: pseae-PA2934 , 9gamm-d0bwk6

Title : Pseudomonas aeruginosa Cif defines a distinct class of alpha\/beta epoxide hydrolases utilizing a His\/Tyr ring-opening pair - Bahl_2012_Protein.Pept.Lett_19_186
Author(s) : Bahl CD , Madden DR
Ref : Protein Pept Lett , 19 :186 , 2012
Abstract : The Gram-negative bacterium Pseudomonas aeruginosa is an opportunistic pathogen that secretes a multitude of virulence factors during the course of infection. Among these is Cif, an epoxide hydrolase (EH) that reduces the functional localization of the cystic fibrosis transmembrane conductance regulator in epithelial cells. In addition to being the first reported EH virulence factor, Cif possesses unique sequence deviations from canonical EH motifs. Foremost among these is the substitution of a histidine for the first epoxide ring-opening tyrosine in the active site. To test the functional equivalence of Tyr and His side chains at this position, we have generated the mutant Cif-H177Y. Structural analysis confirms that both the WT His and mutant Tyr side chains can be accommodated without large-scale conformational changes. However, the Tyr mutant is functionally inactive. Based on a detailed analysis of the structure of the Tyr mutant, it appears that Cif's main-chain conformation imposes a functional requirement for a His at this position. Comparison with canonical EH structures reveals additional conformational differences, which are coupled to divergent sequence characteristics. When used to probe the genomes of other opportunistic pathogens, these sequence-structure criteria uncover candidate sequences that appear to form a distinct subfamily of Cif-like epoxide hydrolases characterized by a conserved His/Tyr ring-opening pair.
ESTHER : Bahl_2012_Protein.Pept.Lett_19_186
PubMedSearch : Bahl_2012_Protein.Pept.Lett_19_186
PubMedID: 21933119
Gene_locus related to this paper: pseae-PA2934

Title : Epoxide-mediated CifR repression of cif gene expression utilizes two binding sites in Pseudomonas aeruginosa - Ballok_2012_J.Bacteriol_194_5315
Author(s) : Ballok AE , Bahl CD , Dolben EL , Lindsay AK , St Laurent JD , Hogan DA , Madden DR , O'Toole GA
Ref : Journal of Bacteriology , 194 :5315 , 2012
Abstract : Pseudomonas aeruginosa secretes an epoxide hydrolase virulence factor that reduces the apical membrane expression of ABC transporters such as the cystic fibrosis transmembrane conductance regulator (CFTR). This virulence factor, named CFTR inhibitory factor (Cif), is regulated by a TetR-family, epoxide-responsive repressor known as CifR via direct binding and repression. We identified two sites of CifR binding in the intergenic space between cifR and morB, the first gene in the operon containing the cif gene. We have mapped these binding sites and found they are 27 bp in length, and they overlap the -10 and +1 sites of both the cifR and morB regulatory region and the start of transcription, respectively. In addition, we found that CifR binds to each repression site with differing affinity. Mutagenesis of these binding sites resulted in a loss of DNA binding in vitro, and mutation of one of these sites in vivo resulted in an increase in transcription of both the cif and cifR genes. We characterized cif and cifR gene expression in sputum and found that, whereas cif gene expression varied relative to an in vitro coculture control, cifR gene expression was consistently higher. Analysis of a longitudinal sample of CF isolates from nine patients revealed that Cif protein was expressed over time, although variably, and these changes could not be linked to mutations in the cifR gene or the promoters of these genes. Finally, we tested CifR responsiveness to other epoxides and showed that CifR can respond to multiple epoxides to various degrees.
ESTHER : Ballok_2012_J.Bacteriol_194_5315
PubMedSearch : Ballok_2012_J.Bacteriol_194_5315
PubMedID: 22843844
Gene_locus related to this paper: pseae-PA2934

Title : Disabled-2 protein facilitates assembly polypeptide-2-independent recruitment of cystic fibrosis transmembrane conductance regulator to endocytic vesicles in polarized human airway epithelial cells - Cihil_2012_J.Biol.Chem_287_15087
Author(s) : Cihil KM , Ellinger P , Fellows A , Stolz DB , Madden DR , Swiatecka-Urban A
Ref : Journal of Biological Chemistry , 287 :15087 , 2012
Abstract : Cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-activated Cl(-) channel expressed in the apical plasma membrane of fluid-transporting epithelia, where the plasma membrane abundance of CFTR is in part controlled by clathrin-mediated endocytosis. The protein networks that control CFTR endocytosis in epithelial cells have only been partially explored. The assembly polypeptide-2 complex (AP-2) is the prototypical endocytic adaptor critical for optimal clathrin coat formation. AP-2 is essential for recruitment of cargo proteins bearing the YXXPhi motif. Although AP-2 interacts directly with CFTR in vitro and facilitates CFTR endocytosis in some cell types, it remains unknown whether it is critical for CFTR uptake into clathrin-coated vesicles (CCVs). Disabled-2 (Dab2) is a clathrin-associated sorting protein (CLASP) that contributes to clathrin recruitment, vesicle formation, and cargo selection. In intestinal epithelial cells Dab2 was not found to play a direct role in CFTR endocytosis. By contrast, AP-2 and Dab2 were shown to facilitate CFTR endocytosis in human airway epithelial cells, although the specific mechanism remains unknown. Our data demonstrate that Dab2 mediates AP-2 independent recruitment of CFTR to CCVs in polarized human airway epithelial cells. As a result, it facilitates CFTR endocytosis and reduces CFTR abundance and stability in the plasma membrane. These effects are mediated by the DAB homology domain. Moreover, we show that in human airway epithelial cells AP-2 is not essential for CFTR recruitment to CCVs.
ESTHER : Cihil_2012_J.Biol.Chem_287_15087
PubMedSearch : Cihil_2012_J.Biol.Chem_287_15087
PubMedID: 22399289

Title : Crystal structure of the CFTR inhibitory factor Cif reveals novel active-site features of an epoxide hydrolase virulence factor. - Bahl_2010_J.Bacteriol_192_1785
Author(s) : Bahl CD , Morisseau C , Bomberger JM , Stanton BA , Hammock BD , O'Toole GA , Madden DR
Ref : Journal of Bacteriology , 192 :1785 , 2010
Abstract : Cystic fibrosis transmembrane conductance regulator (CFTR) inhibitory factor (Cif) is a virulence factor secreted by Pseudomonas aeruginosa that reduces the quantity of CFTR in the apical membrane of human airway epithelial cells. Initial sequence analysis suggested that Cif is an epoxide hydrolase (EH), but its sequence violates two strictly conserved EH motifs and is also compatible with other alpha/beta hydrolase family members with diverse substrate specificities. To investigate the mechanistic basis of Cif activity, we have determined its structure at 1.8 A resolution by X-ray crystallography. The catalytic triad consists of residues Asp129, His297, and Glu153, which are conserved across the family of EHs. At other positions, sequence deviations from canonical EH active-site motifs are stereochemically conservative. Furthermore, detailed enzymatic analysis confirms that Cif catalyzes the hydrolysis of epoxide compounds, with specific activity against both epibromohydrin and cis-stilbene oxide, but with a relatively narrow range of substrate selectivity. Although closely related to two other classes of alpha/beta hydrolase in both sequence and structure, Cif does not exhibit activity as either a haloacetate dehalogenase or a haloalkane dehalogenase. Reassessment of the structural and functional consequences of the H269A mutation suggests that Cif's effect on host-cell CFTR expression may require hydrolysis of an extended endogenous epoxide substrate.
ESTHER : Bahl_2010_J.Bacteriol_192_1785
PubMedSearch : Bahl_2010_J.Bacteriol_192_1785
PubMedID: 20118260
Gene_locus related to this paper: pseae-PA2934

Title : Purification, crystallization and preliminary X-ray diffraction analysis of Cif, a virulence factor secreted by Pseudomonas aeruginosa - Bahl_2010_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_66_26
Author(s) : Bahl CD , Maceachran DP , O'Toole GA , Madden DR
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 66 :26 , 2010
Abstract : The opportunistic pathogen Pseudomonas aeruginosa secretes a protein that triggers the accelerated degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) in airway epithelial cells. This protein, which is known as the CFTR inhibitory factor (Cif), acts as a virulence factor and may facilitate airway colonization by P. aeruginosa. Based on sequence similarity Cif appears to be an epoxide hydrolase (EH), but it lacks several of the conserved features found in the active sites of canonical members of the EH family. Here, the crystallization of purified recombinant Cif by vapor diffusion is reported. The crystals formed in space group C2, with unit-cell parameters a = 167.4, b = 83.6, c = 88.3 A, beta = 100.6 degrees . The crystals diffracted to 2.39 A resolution on a rotating-anode source. Based on the calculated Matthews coefficient (2.2 A(3) Da(-1)), it appears that the asymmetric unit contains four molecules.
ESTHER : Bahl_2010_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_66_26
PubMedSearch : Bahl_2010_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_66_26
PubMedID: 20057063
Gene_locus related to this paper: pseae-PA2934