Matches in SemOpenAlex for { <https://semopenalex.org/work/W3036404410> ?p ?o ?g. }
- W3036404410 abstract "Local structural frustration, the existence of mutually exclusive competing interactions, may explain why some proteins are dynamic while others are rigid. Frustration is thought to underpin biomolecular recognition and the flexibility of protein-binding sites. Here, we show how a small chemical modification, the oxidation of two cysteine thiols to a disulfide bond, during the catalytic cycle of the N-terminal domain of the key bacterial oxidoreductase DsbD (nDsbD), introduces frustration ultimately influencing protein function. In oxidized nDsbD, local frustration disrupts the packing of the protective cap-loop region against the active site allowing loop opening. By contrast, in reduced nDsbD the cap loop is rigid, always protecting the active-site thiols from the oxidizing environment of the periplasm. Our results point toward an intricate coupling between the dynamics of the active-site cysteines and of the cap loop which modulates the association reactions of nDsbD with its partners resulting in optimized protein function." @default.
- W3036404410 created "2020-06-25" @default.
- W3036404410 creator A5001614024 @default.
- W3036404410 creator A5041718990 @default.
- W3036404410 creator A5047204586 @default.
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- W3036404410 creator A5083195797 @default.
- W3036404410 creator A5083309243 @default.
- W3036404410 creator A5088997870 @default.
- W3036404410 creator A5091503896 @default.
- W3036404410 date "2020-06-22" @default.
- W3036404410 modified "2023-09-30" @default.
- W3036404410 title "Local frustration determines loop opening during the catalytic cycle of an oxidoreductase" @default.
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- W3036404410 doi "https://doi.org/10.7554/elife.54661" @default.
- W3036404410 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7347389" @default.
- W3036404410 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32568066" @default.
- W3036404410 hasPublicationYear "2020" @default.
- W3036404410 type Work @default.