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-Structure paper
タイトル | Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 118, Issue 48, Year 2021 |
掲載日 | 2021年11月30日 |
著者 | Eduardo M Bruch / Pierre Vilela / Lu Yang / Alexandra Boyko / Norik Lexa-Sapart / Bertrand Raynal / Pedro M Alzari / Marco Bellinzoni / |
PubMed 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. |
リンク | Proc Natl Acad Sci U S A / PubMed:34819376 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.35 - 3.92 Å |
構造データ | EMDB-11600: PDB-6zzi: PDB-6zzj: PDB-6zzk: PDB-6zzl: PDB-6zzm: PDB-6zzn: |
化合物 | ChemComp-HOH: ChemComp-CAO: ChemComp-EPE: ChemComp-COA: ChemComp-LPM: ChemComp-GOL: ChemComp-PO4: ChemComp-ACT: ChemComp-IMD: |
由来 |
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キーワード | TRANSFERASE / PDH / ODH / acetyltransferase / lipoamide / corynebacterium / CoA / BCKDH / acyltransferase / mycobacterium / tuberculosis |