1QS0

Crystal Structure of Pseudomonas Putida 2-oxoisovalerate Dehydrogenase (Branched-Chain Alpha-Keto Acid Dehydrogenase, E1B)

1QS0 の概要

• エントリーDOI: 10.2210/pdb1qs0/pdb
• 分子名称: 2-OXOISOVALERATE DEHYDROGENASE ALPHA-SUBUNIT, 2-OXOISOVALERATE DEHYDROGENASE BETA-SUBUNIT, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: heterotetramer, thdp cofactor, oxidoreductase
• 由来する生物種: Pseudomonas putida; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83684.04

構造登録者

Aevarsson, A.,Seger, K.,Turley, S.,Sokatch, J.R.,Hol, W.G.J. (登録日: 1999-06-24, 公開日: 1999-08-18, 最終更新日: 2024-11-20)

主引用文献

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

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: 10426958
DOI: 10.1038/11563

実験手法

X-RAY DIFFRACTION (2.4 Å)