1W85
The crystal structure of pyruvate dehydrogenase E1 bound to the peripheral subunit binding domain of E2
Summary for 1W85
| Entry DOI | 10.2210/pdb1w85/pdb |
| Related | 1B5S 1EBD 1LAB 1LAC 1W3D 1W4E 1W4F 1W4G 1W4H 1W88 2PDD 2PDE |
| Descriptor | PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT, PYRUVATE DEHYDROGENASE E1 COMPONENT, BETA SUBUNIT, DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE, ... (8 entities in total) |
| Functional Keywords | pyruvate, dehydrogenase, dihydrolipoyl, acetyl transferase, multienzyme complex, oxidoreductase, transferase |
| Biological source | GEOBACILLUS STEAROTHERMOPHILUS More |
| Total number of polymer chains | 10 |
| Total formula weight | 319851.73 |
| Authors | Frank, R.A.W.,Pratap, J.V.,Pei, X.Y.,Perham, R.N.,Luisi, B.F. (deposition date: 2004-09-16, release date: 2004-11-02, Last modification date: 2023-12-13) |
| Primary citation | Frank, R.A.,Titman, C.M.,Pratap, J.V.,Luisi, B.F.,Perham, R.N. A molecular switch and proton wire synchronize the active sites in thiamine enzymes. Science, 306:872-876, 2004 Cited by PubMed Abstract: 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. PubMed: 15514159DOI: 10.1126/science.1101030 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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