1QS0
Crystal Structure of Pseudomonas Putida 2-oxoisovalerate Dehydrogenase (Branched-Chain Alpha-Keto Acid Dehydrogenase, E1B)
Summary for 1QS0
| Entry DOI | 10.2210/pdb1qs0/pdb |
| Descriptor | 2-OXOISOVALERATE DEHYDROGENASE ALPHA-SUBUNIT, 2-OXOISOVALERATE DEHYDROGENASE BETA-SUBUNIT, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | heterotetramer, thdp cofactor, oxidoreductase |
| Biological source | Pseudomonas putida More |
| Total number of polymer chains | 2 |
| Total formula weight | 83684.04 |
| Authors | Aevarsson, A.,Seger, K.,Turley, S.,Sokatch, J.R.,Hol, W.G.J. (deposition date: 1999-06-24, release date: 1999-08-18, Last modification date: 2024-11-20) |
| Primary citation | Aevarsson, A.,Seger, K.,Turley, S.,Sokatch, J.R.,Hol, W.G. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat.Struct.Biol., 6:785-792, 1999 Cited by PubMed Abstract: The family of giant multienzyme complexes metabolizing pyruvate, 2-oxoglutarate, branched-chain 2-oxo acids or acetoin contains several of the largest and most sophisticated protein assemblies known, with molecular masses between 4 and 10 million Da. The principal enzyme components, E1, E2 and E3, are present in numerous copies and utilize multiple cofactors to catalyze a directed sequence of reactions via substrate channeling. The crystal structure of a heterotetrameric (alpha2beta2) E1, 2-oxoisovalerate dehydrogenase from Pseudomonas putida, reveals a tightly packed arrangement of the four subunits with the beta2-dimer held between the jaws of a 'vise' formed by the alpha2-dimer. A long hydrophobic channel, suitable to accommodate the E2 lipoyl-lysine arm, leads to the active site, which contains the cofactor thiamin diphosphate (ThDP) and an inhibitor-derived covalent modification of a histidine side chain. The E1 structure, together with previous structural information on E2 and E3, completes the picture of the shared architectural features of these enormous macromolecular assemblies. PubMed: 10426958DOI: 10.1038/11563 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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