7JQZ

Crystal structure of Cfl2 wild-type from Burkholderia cenocepacia

Summary for 7JQZ

• Entry DOI: 10.2210/pdb7jqz/pdb
• Related: 7JQX 7JQY
• Descriptor: Alpha/beta hydrolase fold (2 entities in total)
• Functional Keywords: decamer, alpha/beta hydrolase fold, hydrolase
• Biological source: Burkholderia cenocepacia (strain MC0-3)
• Total number of polymer chains: 10
• Total formula weight: 345409.22

Authors

Taher, N.M.,Madden, D.R. (deposition date: 2020-08-11, release date: 2021-03-17, Last modification date: 2023-10-18)

Primary citation

Taher, N.M.,Hvorecny, K.L.,Burke, C.M.,Gilman, M.S.A.,Heussler, G.E.,Adolf-Bryfogle, J.,Bahl, C.D.,O'Toole, G.A.,Madden, D.R.
Biochemical and structural characterization of two cif-like epoxide hydrolases from Burkholderia cenocepacia .
Curr Res Struct Biol, 3:72-84, 2021

PubMed 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 . Although the presence of such Cif-like epoxide hydrolases was predicted in other opportunistic pathogens based on sequence analyses, only Cif and its homolog aCif from have been characterized. Here we report the biochemical and structural characteristics of Cfl1 and Cfl2, two Cif-like epoxide hydrolases from . 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 α/β 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.

PubMed: 34235487
DOI: 10.1016/j.crstbi.2021.02.002

Experimental method

X-RAY DIFFRACTION (2.2 Å)