8P5S

Crystal structure of the homohexameric 2-oxoglutarate dehydrogenase OdhA from Corynebacterium glutamicum

8P5S の概要

• エントリーDOI: 10.2210/pdb8p5s/pdb
• 分子名称: 2-oxoglutarate dehydrogenase E1/E2 component, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, COENZYME A, ... (7 entities in total)
• 機能のキーワード: 2-oxoglutarate dehydrogenase; odh, oxidoreductase
• 由来する生物種: Corynebacterium glutamicum ATCC 13032
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 126775.60

構造登録者

Yang, L.,Boyko, A.,Bellinzoni, M. (登録日: 2023-05-24, 公開日: 2023-08-16, 最終更新日: 2023-08-23)

主引用文献

Yang, L.,Wagner, T.,Mechaly, A.,Boyko, A.,Bruch, E.M.,Megrian, D.,Gubellini, F.,Alzari, P.M.,Bellinzoni, M.
High resolution cryo-EM and crystallographic snapshots of the actinobacterial two-in-one 2-oxoglutarate dehydrogenase.
Nat Commun, 14:4851-4851, 2023

PubMed Abstract: Actinobacteria possess unique ways to regulate the oxoglutarate metabolic node. Contrary to most organisms in which three enzymes compose the 2-oxoglutarate dehydrogenase complex (ODH), actinobacteria rely on a two-in-one protein (OdhA) in which both the oxidative decarboxylation and succinyl transferase steps are carried out by the same polypeptide. Here we describe high-resolution cryo-EM and crystallographic snapshots of representative enzymes from Mycobacterium smegmatis and Corynebacterium glutamicum, showing that OdhA is an 800-kDa homohexamer that assembles into a three-blade propeller shape. The obligate trimeric and dimeric states of the acyltransferase and dehydrogenase domains, respectively, are critical for maintaining the overall assembly, where both domains interact via subtle readjustments of their interfaces. Complexes obtained with substrate analogues, reaction products and allosteric regulators illustrate how these domains operate. Furthermore, we provide additional insights into the phosphorylation-dependent regulation of this enzymatic machinery by the signalling protein OdhI.

PubMed: 37563123
DOI: 10.1038/s41467-023-40253-6

実験手法

X-RAY DIFFRACTION (2.459 Å)