2wvg | pdb_00002wvg

Structural insights into the pre-reaction state of pyruvate decarboxylase from Zymomonas mobilis

spinqualitylabelsall models 2wvg, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wvg is a 4 chain structure with sequence from "achromobacter_anaerobium"_(sic)_shimwell_1937 "achromobacter anaerobium" (sic) shimwell 1937. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: F, MG, TPU Related: 2wvh, 1zpd Activity: Pyruvate decarboxylase, with EC number 4.1.1.1 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 Pyruvate decarboxylase (PDC) uses thiamine diphosphate as an essential cofactor to catalyze the formation of acetaldehyde on the pathway of ethanol synthesis. Here we report the crystallographic image of a prereaction intermediate of a bacterial pyruvate decarboxylase prepared by cocrystallizing the enzyme with pyruvate and a stable analogue of the cofactor's activated ylid form. A second crystal structure of PDC in complex with fluoride shows that the ion organizes a water molecule that occludes the pyruvate binding site, accounting for the inhibitory effect of the halide. Also reported is a structure of the cofactor-free apo form, which when compared to the structure of the holo form indicates how thiamine diphosphate organizes the active site pocket of pyruvate decarboxylase to support catalysis. Guided by the structural and enzymatic data, we propose roles for several key residues in the catalytic mechanism. Structural Insights into the Prereaction State of Pyruvate Decarboxylase from Zymomonas mobilis .,Pei XY, Erixon KM, Luisi BF, Leeper FJ Biochemistry. 2010 Feb 5. PMID:20099870 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pyruvate decarboxylase

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