2YID

Crystal structure of the SucA domain of Mycobacterium smegmatis alpha- ketoglutarate decarboxylase in complex with the enamine-ThDP intermediate

2YID の概要

• エントリーDOI: 10.2210/pdb2yid/pdb
• 関連するPDBエントリー: 2XT6 2XT8 2XT9 2XTA 2Y0P 2YIC
• 分子名称: 2-OXOGLUTARATE DECARBOXYLASE, (4E)-4-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-2(3H)-ylidene}-4-hydroxybutanoic acid, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: lyase, thdp-covalent adduct
• 由来する生物種: MYCOBACTERIUM SMEGMATIS
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 391029.70

構造登録者

Wagner, T.,Bellinzoni, M.,Wehenkel, A.M.,O'Hare, H.M.,Alzari, P.M. (登録日: 2011-05-11, 公開日: 2011-06-15, 最終更新日: 2023-12-20)

主引用文献

Wagner, T.,Bellinzoni, M.,Wehenkel, A.M.,O'Hare, H.M.,Alzari, P.M.
Functional Plasticity and Allosteric Regulation of Alpha-Ketoglutarate Decarboxylase in Central Mycobacterial Metabolism.
Chem.Biol., 18:1011-, 2011

PubMed Abstract: The α-ketoglutarate dehydrogenase (KDH) complex is a major regulatory point of aerobic energy metabolism. Mycobacterium tuberculosis was reported to lack KDH activity, and the putative KDH E1o component, α-ketoglutarate decarboxylase (KGD), was instead assigned as a decarboxylase or carboligase. Here, we show that this protein does in fact sustain KDH activity, as well as the additional two reactions, and these multifunctional properties are shared by the Escherichia coli homolog, SucA. We also show that the mycobacterial enzyme is finely regulated by an additional acyltransferase-like domain and by the action of acetyl-CoA, a powerful allosteric activator able to enhance the concerted protein motions observed during catalysis. Our results uncover the functional plasticity of a crucial node in bacterial metabolism, which may be important for M. tuberculosis during host infection.

PubMed: 21867916
DOI: 10.1016/J.CHEMBIOL.2011.06.004

実験手法

X-RAY DIFFRACTION (2.25 Å)