6ZZK

Crystal structure of the catalytic domain of C. glutamicum AceF (E2p) in ternary complex with CoA and dihydrolipoamide.

6ZZK の概要

• エントリーDOI: 10.2210/pdb6zzk/pdb
• 分子名称: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, COENZYME A, 6,8-DIMERCAPTO-OCTANOIC ACID AMIDE, ... (4 entities in total)
• 機能のキーワード: pdh, odh, acetyltransferase, lipoamide, corynebacterium, coa, transferase
• 由来する生物種: Corynebacterium glutamicum ATCC 13032
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54066.32

構造登録者

Bruch, E.M.,Bellinzoni, M. (登録日: 2020-08-04, 公開日: 2021-08-18, 最終更新日: 2024-01-31)

主引用文献

Bruch, E.M.,Vilela, P.,Yang, L.,Boyko, A.,Lexa-Sapart, N.,Raynal, B.,Alzari, P.M.,Bellinzoni, M.
Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: 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.

PubMed: 34819376
DOI: 10.1073/pnas.2112107118

実験手法

X-RAY DIFFRACTION (2.09 Å)