ArticleBiochemistry2019
Crystal Structure and Conformational Dynamics of Pyrococcus furiosus Prolyl Oligopeptidase.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Structural basis for dimerization, catalytic regulation, and substrate selectivity of the chloroplast S9D CGEP protease in Arabidopsis thaliana.Protein science : a publication of the Protein Society · 2026Article
- Mechanistic Insight into Conformational Control of Enzyme Activity by Genetically Encoded Metal-Responsive Switches.Chembiochem : a European journal of chemical biology · 2026Article
- Structural basis for dimerization, catalytic regulation, and substrate selectivity in S9D proteases.bioRxiv : the preprint server for biology · 2026Article
- Structure-Based Identification of Non-covalent Prolyl Oligopeptidase 80 Inhibitors TargetingJournal of chemical information and modeling · 2025Article
- Noncanonical Amino Acids: Bringing New-to-Nature Functionalities to Biocatalysis.Chemical reviews · 2024Review
- Comparative analysis of thermal adaptations of extremophilic prolyl oligopeptidases.Biophysical journal · 2024Article
- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
- Iridium(III) polypyridine artificial metalloenzymes with tunable photophysical properties: a new platform for visible light photocatalysis in aqueous solution.Dalton transactions (Cambridge, England : 2003) · 2023Article
- Crystal Structure of Inhibitor-Bound Bacterial Oligopeptidase B in the Closed State: Similarity and Difference between Protozoan and Bacterial Enzymes.International journal of molecular sciences · 2023Article
- Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications.Plants (Basel, Switzerland) · 2022Review
- Metal-responsive regulation of enzyme catalysis using genetically encoded chemical switches.Nature communications · 2022Article
- Controlling the optical and catalytic properties of artificial metalloenzyme photocatalysts using chemogenetic engineering.Chemical science · 2022Article
- Multiple conserved states characterize the twist landscape of the bacterial actin homolog MreB.Computational and structural biotechnology journal · 2022Article
- Article
- Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus.Scientific reports · 2021Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Enzymes in the prolyl oligopeptidase family possess unique structures and substrate specificities that are important for their biological activity and for potential biocatalytic applications. The crystal structures of Pyrococcus furiosus ( Pfu) prolyl oligopeptidase (POP) and the corresponding S477C mutant were determined to 1.9 and 2.2 Å resolution, respectively. The wild type enzyme crystallized in an open conformation, indicating that this state is readily accessible, and it contained bound chloride ions and a prolylproline ligand. These structures were used as starting points for molecular dynamics simulations of Pfu POP conformational dynamics. The simulations showed that large-scale domain opening and closing occurred spontaneously, providing facile substrate access to the active site. Movement of the loop containing the catalytically essential histidine into a conformation similar to those found in structures with fully formed catalytic triads also occurred. This movement was modulated by chloride binding, providing a rationale for experimentally observed activation of POP peptidase catalysis by chloride. Thus, the structures and simulations reported in this study, combined with existing biochemical data, provide a number of insights into POP catalysis.
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