2dji | pdb_00002dji

Crystal Structure of Pyruvate Oxidase from Aerococcus viridans containing FAD

spinqualitylabelsall models 2dji, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2dji is a 1 chain structure with sequence from "gaffkya_homari"_hitchner_and_snieszko_1947 "gaffkya homari" hitchner and snieszko 1947. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, SO4 Related: 1v5e, 1v5f, 1v5g, 1pox Activity: Pyruvate oxidase, with EC number 1.2.3.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structures of pyruvate oxidase from Aerococcus viridans (AvPOX) complexed with flavin adenine dinucleotide (FAD), with FAD and thiamine diphosphate (ThDP) and with FAD and the 2-acetyl-ThDP intermediate (AcThDP) have been determined at 1.6, 1.8 and 1.9 A resolution, respectively. Each subunit of the homotetrameric AvPOX enzyme consists of three domains, as observed in other ThDP-dependent enzymes. FAD is bound within one subunit in the elongated conformation and with the flavin moiety being planar in the oxidized form, while ThDP is bound in a conserved V-conformation at the subunit-subunit interface. The structures reveal flexible regions in the active-site tunnel which may undergo conformational changes to allow the entrance of the substrates and the exit of the reaction products. Of particular interest is the role of Lys478, the side chain of which may be bent or extended depending on the stage of catalysis. The structures also provide insight into the routes for electron transfer to FAD and the involvement of active-site residues in the catalysis of pyruvate to its products. The structures of pyruvate oxidase from Aerococcus viridans with cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysis.,Juan EC, Hoque MM, Hossain MT, Yamamoto T, Imamura S, Suzuki K, Sekiguchi T, Takenaka A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt, 11):900-7. Epub 2007 Oct 20. PMID:18007037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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