1w85
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THE CRYSTAL STRUCTURE OF PYRUVATE DEHYDROGENASE E1 BOUND TO THE PERIPHERAL SUBUNIT BINDING DOMAIN OF E2
OverviewOverview
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 StructureAbout this Structure
1W85 is a Protein complex structure of sequences from Geobacillus stearothermophilus with MG, K, TDP and PEG as ligands. Active as Pyruvate dehydrogenase (acetyl-transferring), with EC number 1.2.4.1 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
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
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