2JGD
E. COLI 2-oxoglutarate dehydrogenase (E1o)
2JGD の概要
| エントリーDOI | 10.2210/pdb2jgd/pdb |
| 分子名称 | 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT, ADENOSINE MONOPHOSPHATE, ... (4 entities in total) |
| 機能のキーワード | 2-oxoglutarate dehydrogenase, flavoprotein, oxidoreductase, thiamine diphosphate, thiamine pyrophosphate, adenosine monophosphate, e1o, kgdh, ogdh, glycolysis, oxaloacetate |
| 由来する生物種 | ESCHERICHIA COLI 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 211074.85 |
| 構造登録者 | Frank, R.A.W.,Price, A.J.,Northrop, F.D.,Perham, R.N.,Luisi, B.F. (登録日: 2007-02-12, 公開日: 2007-02-27, 最終更新日: 2024-05-08) |
| 主引用文献 | Frank, R.A.W.,Price, A.J.,Northrop, F.D.,Perham, R.N.,Luisi, B.F. Crystal Structure of the E1 Component of the Escherichia Coli 2-Oxoglutarate Dehydrogenase Multienzyme Complex. J.Mol.Biol., 368:639-, 2007 Cited by PubMed Abstract: The thiamine-dependent E1o component (EC 1.2.4.2) of the 2-oxoglutarate dehydrogenase complex catalyses a rate-limiting step of the tricarboxylic acid cycle (TCA) of aerobically respiring organisms. We describe the crystal structure of Escherichia coli E1o in its apo and holo forms at 2.6 A and 3.5 A resolution, respectively. The structures reveal the characteristic fold that binds thiamine diphosphate and resemble closely the alpha(2)beta(2) hetero-tetrameric E1 components of other 2-oxo acid dehydrogenase complexes, except that in E1o, the alpha and beta subunits are fused as a single polypeptide. The extended segment that links the alpha-like and beta-like domains forms a pocket occupied by AMP, which is recognised specifically. Also distinctive to E1o are N-terminal extensions to the core fold, and which may mediate interactions with other components of the 2-oxoglutarate dehydrogenase multienzyme complex. The active site pocket contains a group of three histidine residues and one serine that appear to confer substrate specificity and the capacity to accommodate the TCA metabolite oxaloacetate. Oxaloacetate inhibits E1o activity at physiological concentrations, and we suggest that the inhibition may allow coordinated activity within the TCA cycle. We discuss the implications for metabolic control in facultative anaerobes, and for energy homeostasis of the mammalian brain. PubMed: 17367808DOI: 10.1016/J.JMB.2007.01.080 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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