1w88
From Proteopedia
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THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1(D180N, E183Q) BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2
Overview
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.
About this Structure
1W88 is a Protein complex structure of sequences from Geobacillus stearothermophilus with and as ligands. Active as Pyruvate dehydrogenase (acetyl-transferring), with EC number 1.2.4.1 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:41:30 2008
Categories: Geobacillus stearothermophilus | Protein complex | Pyruvate dehydrogenase (acetyl-transferring) | Frank, R A.W. | Luisi, B F. | Pei, X Y. | Perham, R N. | Pratap, J V. | MG | TDP | Acetyl transferase | Catalysis | Dihydrolipoyl | Multienzyme complex | Oxidoreductase | Pyruvate dehydrogenase | Slinky | Transferase
