ArticleStructure (London, England : 1993)2017
Active-Site Flexibility and Substrate Specificity in a Bacterial Virulence Factor: Crystallographic Snapshots of an Epoxide Hydrolase.
Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Convergent strategies for nanobody-mediated inhibition of an epoxide hydrolase.bioRxiv : the preprint server for biology · 2026Article
- Review
- Evolution of tunnels in α/β-hydrolase fold proteins-What can we learn from studying epoxide hydrolases?PLoS computational biology · 2022Article
- Biochemical and structural characterization of two cif-like epoxide hydrolases fromCurrent research in structural biology · 2021Article
- Mutation of an atypical oxirane oxyanion hole improves regioselectivity of the α/β-fold epoxide hydrolase Alp1U.The Journal of biological chemistry · 2020Article
- Substrate structure and computation guided engineering of a lipase for omega-3 fatty acid selectivity.PloS one · 2020Article
- Ligand Binding Site Structure Influences the Evolution of Protein Complex Function and Topology.Cell reports · 2018Article
- An epoxide hydrolase secreted by Pseudomonas aeruginosa decreases mucociliary transport and hinders bacterial clearance from the lung.American journal of physiology. Lung cellular and molecular physiology · 2018Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
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 α/β-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.
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