6csj

Structure of a Bacillus coagulans polyol dehydrogenase double mutant with an acquired D-lactate dehydrogenase activity

spinqualitylabelsall models 6csj, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6csj is a 8 chain structure with sequence from Weizmannia coagulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.395Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A150JSL8_WEICA Publication Abstract from PubMed During adaptive metabolic evolution a native glycerol dehydrogenase (GDH) acquired a d-lactate dehydrogenase (LDH) activity. Two active-site amino acid changes were detected in the altered protein. Biochemical studies along with comparative structure analysis using an X-ray crystallographic structure model of the protein with the two different amino acids allowed prediction of pyruvate binding into the active site. We propose that the F245S alteration increased the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 gamma-O and the C1 carboxylate of pyruvate. To our knowledge, this is the first GDH to gain LDH activity due to an active site amino acid change, a desired result of in vivo enzyme evolution. Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d-lactate dehydrogenase activity.,Chauliac D, Wang Q, St John FJ, Jones G, Hurlbert JC, Ingram LO, Shanmugam KT Protein Sci. 2020 Dec;29(12):2387-2397. doi: 10.1002/pro.3963. Epub 2020 Oct 24. PMID:33020946 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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