Taher_2021_Curr.Res.Struct.Biol_3_72

Reference

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.

PubMedSearch : Taher_2021_Curr.Res.Struct.Biol_3_72
PubMedID: 34235487
Gene_locus related to this paper: burch-a0az59 , burch-a0b0f8

Related information

Gene_locus burch-a0az59    burch-a0b0f8
Structure burch-a0az59    burch-a0b0f8    7JQX    7JQY    7JQZ

Citations formats

Taher NM, Hvorecny KL, Burke CM, Gilman MSA, Heussler GE, Adolf-Bryfogle J, Bahl CD, O'Tool GA, Madden DR (2021)
Biochemical and Structural Characterization of Two Cif-Like Epoxide Hydrolases from Burkholderia cenocepacia
Current Research in Structural Biology 3 :72

Taher NM, Hvorecny KL, Burke CM, Gilman MSA, Heussler GE, Adolf-Bryfogle J, Bahl CD, O'Tool GA, Madden DR (2021)
Current Research in Structural Biology 3 :72