Jiang YL

References (6)

Title : Structural and biochemical analyses of the tetrameric carboxypeptidase S9Cfn from Fusobacterium nucleatum - Wang_2021_Acta.Crystallogr.D.Struct.Biol_77_1554
Author(s) : Wang X , Cheng MT , Chen ZP , Jiang YL , Ge YS , Xia R , Hou WT
Ref : Acta Crystallographica D Struct Biol , 77 :1554 , 2021
Abstract : As one of the most abundant bacteria in the human oral cavity, Fusobacterium nucleatum is closely involved in various oral diseases and is also a risk factor for other diseases. The peptidases of F. nucleatum can digest exogenous peptides into amino acids to satisfy its nutrient requirements. Here, a putative F. nucleatum peptidase, termed S9Cfn, which belongs to the S9C peptidase family was identified. Enzymatic activity assays combined with mass-spectrometric analysis revealed that S9Cfn is a carboxypeptidase, but not an aminopeptidase as previously annotated. The crystal structure of the S9Cfn tetramer was solved at 2.6A resolution and was found to contain a pair of oligomeric pores in the center. Structural analysis, together with site-directed mutagenesis and enzymatic activity assays, revealed a substrate-entrance tunnel that extends from each oligomeric pore to the catalytic triad, adjacent to which three conserved arginine residues are responsible for substrate binding. Moreover, comparison with other S9 peptidase structures indicated drastic conformational changes of the oligomeric pores during the catalytic cycle. Together, these findings increase the knowledge of this unique type of tetrameric carboxypeptidase and provide insight into the homeostatic control of microbiota in the human oral cavity.
ESTHER : Wang_2021_Acta.Crystallogr.D.Struct.Biol_77_1554
PubMedSearch : Wang_2021_Acta.Crystallogr.D.Struct.Biol_77_1554
PubMedID: 34866611
Gene_locus related to this paper: fusnu-a0a1s1mbe1

Title : Structural and functional insights into the Asp1\/2\/3 complex mediated secretion of pneumococcal serine-rich repeat protein PsrP - Guo_2020_Biochem.Biophys.Res.Commun_524_784
Author(s) : Guo C , Feng Z , Zuo G , Jiang YL , Zhou CZ , Chen Y , Hou WT
Ref : Biochemical & Biophysical Research Communications , 524 :784 , 2020
Abstract : The accessory sec system consisting of seven conserved components is commonly distributed among pathogenic Gram-positive bacteria for the secretion of serine-rich-repeat proteins (SRRPs). Asp1/2/3 protein complex in the system is responsible for both the O-acetylation of GlcNAc and delivering SRRPs to SecA2. However, the molecular mechanism of how Asp1/2/3 transport SRRPs remains unknown. Here, we report the complex structure of Asp1/2/3 from Streptococcus pneumoniae at 2.9 A. Further functional assays indicated that Asp1/2/3 can stimulate the ATPase activity of SecA2. In addition, the deletion of asp1/2/3 gene resulted in the accumulation of a secreted version of PsrP with an altered glycoform in protoplast fraction of the mutant cell, which suggested the modification/transport coupling of the substrate. Altogether, these findings not only provide structural basis for further investigations on the transport process of SRRPs, but also uncover the indispensable role of Asp1/2/3 in the accessory sec system.
ESTHER : Guo_2020_Biochem.Biophys.Res.Commun_524_784
PubMedSearch : Guo_2020_Biochem.Biophys.Res.Commun_524_784
PubMedID: 32037091
Gene_locus related to this paper: stree-a0a0b7mbs7

Title : Crystallization and preliminary X-ray diffraction analysis of a putative carbon-carbon bond hydrolase from Mycobacterium abscessus 103 - Zhang_2015_Acta.Crystallogr.F.Struct.Biol.Commun_71_239
Author(s) : Zhang Z , Jiang YL , Wu Y , He YX
Ref : Acta Crystallographica F Struct Biol Commun , 71 :239 , 2015
Abstract : The PhlG protein from Mycobacterium abscessus 103 (mPhlG), which shares 30% sequence identity with phloretin hydrolase from Eubacterium ramulus and 38% sequence identity with 2,4-diacetylphloroglucinol hydrolase from Pseudomonas fluorescens Pf-5, is a putative carbon-carbon bond hydrolase. Here, the expression, purification and crystallization of mPhlG are reported. Crystals were obtained using a precipitant consisting of 100 mM citric acid pH 5.0, 1.0 M lithium chloride, 8%(w/v) polyethylene glycol 6000. The crystals diffracted to 1.87 A resolution and belonged to space group P21, with unit-cell parameters a = 71.0, b = 63.4, c = 74.7 A, alpha = 90.0, beta = 103.2, gamma = 90.0 degrees . Assuming the presence of two mPhlG molecules in the asymmetric unit, VM was calculated to be 2.5 A(3) Da(-1), which corresponds to a solvent content of 50%.
ESTHER : Zhang_2015_Acta.Crystallogr.F.Struct.Biol.Commun_71_239
PubMedSearch : Zhang_2015_Acta.Crystallogr.F.Struct.Biol.Commun_71_239
PubMedID: 25664803

Title : Crystal structure of juvenile hormone epoxide hydrolase from the silkworm Bombyx mori - Zhou_2014_Proteins_82_3224
Author(s) : Zhou K , Jia N , Hu C , Jiang YL , Yang JP , Chen Y , Li S , Li WF , Zhou CZ
Ref : Proteins , 82 :3224 , 2014
Abstract : The juvenile hormone (JH) epoxide hydrolase (JHEH) catalyzes the degradation of JH, which regulates the metamorphosis development of insects. Here we report the 2.30 A crystal structure of JHEH from the silkworm Bombyx mori (BmJHEH). The overall structure of BmJHEH is composed of an N-terminal segment followed by a core hydrolase domain, which is interrupted by an all-alpha lid domain. Structural analyses together with molecular simulation reveal insights into the conservation and specificity of the active-site pocket. These findings increase our understanding of the substrate recognition and catalysis of microsomal epoxide hydrolase family and might help the design of JH-derived pesticides. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.
ESTHER : Zhou_2014_Proteins_82_3224
PubMedSearch : Zhou_2014_Proteins_82_3224
PubMedID: 25143157
Gene_locus related to this paper: bommo-q6u6j0

Title : Identification of oxidized protein hydrolase as a potential prodrug target in prostate cancer - McGoldrick_2014_BMC.Cancer_14_77
Author(s) : McGoldrick CA , Jiang YL , Paromov V , Brannon M , Krishnan K , Stone WL
Ref : BMC Cancer , 14 :77 , 2014
Abstract : BACKGROUND: Esterases are often overexpressed in cancer cells and can have chiral specificities different from that of the corresponding normal tissues. For this reason, ester prodrugs could be a promising approach in chemotherapy. In this study, we focused on the identification and characterization of differentially expressed esterases between non-tumorigenic and tumorigenic prostate epithelial cells. METHODS: Cellular lysates from LNCaP, DU 145, and PC3 prostate cancer cell lines, tumorigenic RWPE-2 prostate epithelial cells, and non-tumorigenic RWPE-1 prostate epithelial cells were separated by native polyacrylamide gel electrophoresis (n-PAGE) and the esterase activity bands visualized using alpha-naphthyl acetate or alpha-naphthyl-N-acetylalaninate (ANAA) chiral esters and Fast Blue RR salt. The esterases were identified using nanospray LC/MS-MS tandem mass spectrometry and confirmed by Western blotting, native electroblotting, inhibition assays, and activity towards a known specific substrate. The serine protease/esterase oxidized protein hydrolase (OPH) was overexpressed in COS-7 cells to verify our results. RESULTS: The major esterase observed with the ANAA substrates within the n-PAGE activity bands was identified as OPH. OPH (EC is a serine protease/esterase and a member of the prolyl oligopeptidase family. We found that LNCaP lysates contained approximately 40% more OPH compared to RWPE-1 lysates. RWPE-2, DU145 and PC3 cell lysates had similar levels of OPH activity. OPH within all of the cell lysates tested had a chiral preference for the S-isomer of ANAA. LNCaP cells were stained more intensely with ANAA substrates than RWPE-1 cells and COS-7 cells overexpressing OPH were found to have a higher activity towards the ANAA and AcApNA than parent COS-7 cells. CONCLUSIONS: These data suggest that prodrug derivatives of ANAA and AcApNA could have potential as chemotherapeutic agents for the treatment of prostate cancer tumors that overexpress OPH.
ESTHER : McGoldrick_2014_BMC.Cancer_14_77
PubMedSearch : McGoldrick_2014_BMC.Cancer_14_77
PubMedID: 24512522

Title : A specific molecular beacon probe for the detection of human prostate cancer cells - Jiang_2012_Bioorg.Med.Chem.Lett_22_3632
Author(s) : Jiang YL , McGoldrick CA , Yin D , Zhao J , Patel V , Brannon MF , Lightner JW , Krishnan K , Stone WL
Ref : Bioorganic & Medicinal Chemistry Lett , 22 :3632 , 2012
Abstract : The small-molecule, water-soluble molecular beacon probe 1 is hydrolyzed by the lysate and living cells of human prostate cancer cell lines (LNCaP), resulting in strong green fluorescence. In contrast, probe 1 does not undergo significant hydrolysis in either the lysate or living cells of human nontumorigenic prostate cells (RWPE-1). These results, corroborated by UV-Vis spectroscopy and fluorescent microscopy, reveal that probe 1 is a sensitive and specific fluorogenic and chromogenic sensor for the detection of human prostate cancer cells among nontumorigenic prostate cells and that carboxylesterase activity is a specific biomarker for human prostate cancer cells.
ESTHER : Jiang_2012_Bioorg.Med.Chem.Lett_22_3632
PubMedSearch : Jiang_2012_Bioorg.Med.Chem.Lett_22_3632
PubMedID: 22572577