6ah7

D45W/H226G mutant of marine bacterial prolidase

spinqualitylabelsall models 6ah7, resolution 2.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ah7 is a 4 chain structure with sequence from Pseudoalteromonas lipolytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.38Å Ligands: MN, NA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1I7CHQ2_9GAMM Splits dipeptides with a prolyl residue in the C-terminal position.[HAMAP-Rule:MF_01279][SAAS:SAAS01095084] Publication Abstract from PubMed Enzyme promiscuity is critical to the acquisition of evolutionary plasticity in cells and can be recruited for high-value chemical synthesis or xenobiotic degradation. The molecular determinants of substrate ambiguity are essential to this activity; however, these details remain unknown. Here, we performed the directed evolution of a prolidase to enhance its initially weak paraoxonase activity. The in vitro evolution led to an unexpected 1,000,000-fold switch in substrate selectivity, with a 30-fold increase in paraoxon hydrolysis and 40,000-fold decrease in peptide hydrolysis. Structural and in silico analyses revealed enlarged catalytic cavities and substrate repositioning as responsible for rapid catalytic transitions between distinct chemical reactions. Repurposing a bacterial prolidase for organophosphorus hydrolysis: Reshaped catalytic cavity switches substrate selectivity.,Yang J, Xiao YZ, Li R, Liu Y, Long LJ Biotechnol Bioeng. 2020 Sep;117(9):2694-2702. doi: 10.1002/bit.27455. Epub 2020, Jun 26. PMID:32515491 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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