5hop

1.65 Angstrom resolution crystal structure of lmo0182 (residues 1-245) from Listeria monocytogenes EGD-e

spinqualitylabelsall models 5hop, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5hop is a 2 chain structure with sequence from Listeria monocytogenes EGD-e. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: ACT, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8YAE8_LISMO 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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