8h09

Structure of the thermolabile hemolysin from Vibrio alginolyticus (apo form)

spinqualitylabelsall models 8h09, resolution 1.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8h09 is a 2 chain structure with sequence from Vibrio alginolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.81Å Ligands: 1PE, 1PS, MG, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A7Y4B3E8_VIBAL Publication Abstract from PubMed Although enzyme catalysis is typified by high specificity, enzymes can catalyze various substrates (substrate promiscuity) and/or different reaction types (catalytic promiscuity) using a single active site. This interesting phenomenon is widely distributed in enzyme catalysis, with both fundamental and applied importance. To date, the mechanistic understanding of enzyme promiscuity is very limited. Herein, we report the structural mechanism underlying the substrate and catalytic promiscuity of Vibrio dual lipase/transferase (VDLT). Crystal structures of the VDLT from Vibrio alginolyticus (ValDLT) and its fatty acid complexes were solved, revealing prominent structural flexibility. In particular, the "Ser-His-Asp" catalytic triad machinery of ValDLT contains an intrinsically flexible oxyanion hole. Analysis of ligand-bound structures and mutagenesis showed that the flexible oxyanion hole and other binding residues can undergo distinct conformational changes to facilitate substrate and catalytic promiscuity. Our study reveals a previously unknown flexible form of the famous catalytic triad machinery and proposes a "catalytic site tuning" mechanism to expand the mechanistic paradigm of enzyme promiscuity. Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase.,Wang C, Liu C, Zhu X, Peng Q, Ma Q Nat Commun. 2023 Aug 9;14(1):4795. doi: 10.1038/s41467-023-40455-y. PMID:37558668 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA