3pl8

Pyranose 2-oxidase H167A complex with 3-deoxy-3-fluoro-beta-D-glucose

spinqualitylabelsall models 3pl8, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pl8 is a 1 chain structure with sequence from Trametes ochracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.35Å Ligands: FAD, G3F, MES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7ZA32_TRAOC Publication Abstract from PubMed Trametes multicolor pyranose 2-oxidase (P2O) is a flavoprotein oxidase that oxidizes d-glucose at C2 to 2-keto-d-glucose by a highly regioselective mechanism. In this work, fluorinated sugar substrates were used as mechanistic probes to investigate the basis of regioselectivity in P2O. Although frequently used to study the mechanisms of glycoside hydrolases, our work provides the first example of applying these probes to sugar oxidoreductases. Our previous structure of the P2O mutant H167A in complex with the slow substrate 2-deoxy-2-fluoro-d-glucose showed a substrate-binding mode compatible with oxidation at C3. To accommodate the sugar, a gating segment, (454)FSY(456), in the substrate recognition loop partly unfolded to create a spacious and more polar active site that is distinct from the closed state of P2O. The crystal structure presented here shows that the preferred C2 oxidation where an ordered complex of P2O H167A with 3-deoxy-3-fluoro-d-glucose at 1.35 A resolution was successfully trapped. In this semi-open C2-oxidation complex, the substrate recognition loop tightens to form an optimized substrate complex stabilized by interactions between Asp452 and glucose O4, as well as Tyr456 and the glucose O6 group, interactions that are not possible when glucose is positioned for oxidation at C3. The different conformations of the (454)FSY(456) gating segment in the semi-open and closed states induce backbone and side-chain movements of Thr169 and Asp452 that add further differential stabilization to the individual states. We expect the semi-open state (C2-oxidation state) and closed state to be good approximations of the active-site structure during the reductive half-reaction (sugar oxidation) and oxidative half-reaction (O(2) reduction). Regioselective control of beta-d-glucose oxidation by pyranose 2-oxidase is intimately coupled to conformational degeneracy.,Tan TC, Haltrich D, Divne C J Mol Biol. 2011 Jun 17;409(4):588-600. Epub 2011 Apr 15. PMID:21515286 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pyranose oxidase

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