- EMDB-11600: Cubic core of the dihydrolipoamide acyltransferase (E2b) componen... -
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基本情報
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データベース: EMDB / ID: EMD-11600
タイトル
Cubic core of the dihydrolipoamide acyltransferase (E2b) component of the branched-chain alpha-ketoacid dehydrogenase complex (BCKDH) from M. tuberculosis
マップデータ
CryoEM sharpened map obtained from Crysoparc
試料
複合体: Catalytic domain of M. tuberculosis E2b (acyltransferase from branched-chain alpha-ketoacid dehydrogenase complex)
ジャーナル: Proc Natl Acad Sci U S A / 年: 2021 タイトル: Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex. 著者: Eduardo M Bruch / Pierre Vilela / Lu Yang / Alexandra Boyko / Norik Lexa-Sapart / Bertrand Raynal / Pedro M Alzari / Marco Bellinzoni / 要旨: α-oxoacid dehydrogenase complexes are large, tripartite enzymatic machineries carrying out key reactions in central metabolism. Extremely conserved across the tree of life, they have been, so far, ...α-oxoacid dehydrogenase complexes are large, tripartite enzymatic machineries carrying out key reactions in central metabolism. Extremely conserved across the tree of life, they have been, so far, all considered to be structured around a high-molecular weight hollow core, consisting of up to 60 subunits of the acyltransferase component. We provide here evidence that Actinobacteria break the rule by possessing an acetyltranferase component reduced to its minimally active, trimeric unit, characterized by a unique C-terminal helix bearing an actinobacterial specific insertion that precludes larger protein oligomerization. This particular feature, together with the presence of an gene coding for both the decarboxylase and the acyltransferase domains on the same polypetide, is spread over Actinobacteria and reflects the association of PDH and ODH into a single physical complex. Considering the central role of the pyruvate and 2-oxoglutarate nodes in central metabolism, our findings pave the way to both therapeutic and metabolic engineering applications.