5i0g

Cycloalternan-degrading enzyme from Trueperella pyogenes in complex with cycloalternan

spinqualitylabelsall models 5i0g, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5i0g is a 1 chain structure with sequence from "bacillus_pyogenes"_glage_1903 "bacillus pyogenes" glage 1903. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GLC, SIN Gene: CQ11_05330 ("Bacillus pyogenes" Glage 1903) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Active in the aqueous cellular environment where a massive excess of water is perpetually present, enzymes that catalyze the transfer of an electrophile to a non-water nucleophile (transferases) require specific strategies to inhibit mechanistically related hydrolysis reactions. To identify principles that confer transferase versus hydrolase reaction specificity, we exploited two enzymes that use highly similar catalytic apparatuses to catalyze the transglycosylation (a transferase reaction) or hydrolysis of alpha-1,3-glucan linkages in the cyclic tetrasaccharide cycloalternan (CA). We show that substrate binding to non-catalytic domains and a conformationally stable active site promote CA transglycosylation, whereas a distinct pattern of active site conformational change is associated with CA hydrolysis. These findings defy the classic view of induced-fit conformational change and illustrate a mechanism by which a stable hydrophobic binding site can favor transferase activity and disfavor hydrolysis. Application of these principles could facilitate the rational reengineering of transferases with desired catalytic properties. Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity.,Light SH, Cahoon LA, Mahasenan KV, Lee M, Boggess B, Halavaty AS, Mobashery S, Freitag NE, Anderson WF Structure. 2017 Jan 5. pii: S0969-2126(16)30397-5. doi:, 10.1016/j.str.2016.12.007. PMID:28089449 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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