3dva | pdb_00003dva

Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex

spinqualitylabelsall models 3dva, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dva is a 10 chain structure with sequence from Atcc 12980. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: K, MG, TPW Related: 1w85, 1w88, 3duf, 3dv0 Gene: pdhA (ATCC 12980), pdhB (ATCC 12980), pdhC (ATCC 12980) Activity: Pyruvate dehydrogenase (acetyl-transferring), with EC number 1.2.4.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ODP2_GEOSE] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). [ODPB_GEOSE] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). 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 pyruvate dehydrogenase multienzyme assembly (PDH) generates acetyl coenzyme A and reducing equivalents from pyruvate in a multiple-step process that is a nexus of central metabolism. We report crystal structures of the Geobacillus stearothermophilus PDH E1p subunit with ligands that mimic the prereaction complex and the postdecarboxylation product. The structures implicate residues that help to orient substrates, nurture intermediates, and organize surface loops so that they can engage a mobile lipoyl domain that receives the acetyl group and shuttles it to the next active site. The structural and enzymatic data suggest that H128beta performs a dual role: first, as electrostatic catalyst of the reaction of pyruvate with the thiamine cofactor; and second, as a proton donor in the second reaction of acetyl group with the lipoate. We also identify I206alpha as a key residue in mediating the conformation of active-site loops. We propose that a simple conformational flip of the H271alpha side chain assists transfer of the acetyl group from thiamine cofactor to lipoyl domain in synchrony with reduction of the dithiolane ring. Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multienzyme complex.,Pei XY, Titman CM, Frank RA, Leeper FJ, Luisi BF Structure. 2008 Dec 12;16(12):1860-72. PMID:19081062 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dihydrolipoamide acetyltransferase Pyruvate dehydrogenase 3D structures

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