1w85 | pdb_00001w85

The crystal structure of pyruvate dehydrogenase E1 bound to the peripheral subunit binding domain of E2

spinqualitylabelsall models 1w85, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1w85 is a 10 chain structure with sequence from Atcc 12980. The September 2012 RCSB PDB Molecule of the Month feature on Pyruvate Dehydrogenase Complex by David Goodsell is 10.2210/rcsb_pdb/mom_2012_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: K, MG, PEG, TDP Related: 1b5s, 1ebd, 1lab, 1lac, 1w3d, 1w4e, 1w4f, 1w4g, 1w4h, 1w88, 2pdd, 2pde 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 Thiamine diphosphate (ThDP) is used as a cofactor in many key metabolic enzymes. We present evidence that the ThDPs in the two active sites of the E1 (EC 1.2.4.1) component of the pyruvate dehydrogenase complex communicate over a distance of 20 angstroms by reversibly shuttling a proton through an acidic tunnel in the protein. This "proton wire" permits the co-factors to serve reciprocally as general acid/base in catalysis and to switch the conformation of crucial active-site peptide loops. This synchronizes the progression of chemical events and can account for the oligomeric organization, conformational asymmetry, and "ping-pong" kinetic properties of E1 and other thiamine-dependent enzymes. A molecular switch and proton wire synchronize the active sites in thiamine enzymes.,Frank RA, Titman CM, Pratap JV, Luisi BF, Perham RN Science. 2004 Oct 29;306(5697):872-6. PMID:15514159 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dihydrolipoamide acetyltransferase Pyruvate dehydrogenase

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