7BGJ

C. thermophilum Pyruvate Dehydrogenase Complex Core

7BGJ の概要

• エントリーDOI: 10.2210/pdb7bgj/pdb
• EMDBエントリー: 12181
• 分子名称: Acetyltransferase component of pyruvate dehydrogenase complex (1 entity in total)
• 機能のキーワード: dihydrolipoyl, transacetylase, e2, pyruvate, transferase
• 由来する生物種: Chaetomium thermophilum var. thermophilum DSM 1495
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48777.49

構造登録者

Tueting, C.,Kastritis, P.L. (登録日: 2021-01-07, 公開日: 2021-02-10, 最終更新日: 2024-05-01)

主引用文献

Kyrilis, F.L.,Semchonok, D.A.,Skalidis, I.,Tuting, C.,Hamdi, F.,O'Reilly, F.J.,Rappsilber, J.,Kastritis, P.L.
Integrative structure of a 10-megadalton eukaryotic pyruvate dehydrogenase complex from native cell extracts.
Cell Rep, 34:108727-108727, 2021

PubMed Abstract: The pyruvate dehydrogenase complex (PDHc) is a giant enzymatic assembly involved in pyruvate oxidation. PDHc components have been characterized in isolation, but the complex's quaternary structure has remained elusive due to sheer size, heterogeneity, and plasticity. Here, we identify fully assembled Chaetomium thermophilum α-keto acid dehydrogenase complexes in native cell extracts and characterize their domain arrangements utilizing mass spectrometry, activity assays, crosslinking, electron microscopy (EM), and computational modeling. We report the cryo-EM structure of the PDHc core and observe unique features of the previously unknown native state. The asymmetric reconstruction of the 10-MDa PDHc resolves spatial proximity of its components, agrees with stoichiometric data (60 E2p:12 E3BP:∼20 E1p: ≤ 12 E3), and proposes a minimum reaction path among component enzymes. The PDHc shows the presence of a dynamic pyruvate oxidation compartment, organized by core and peripheral protein species. Our data provide a framework for further understanding PDHc and α-keto acid dehydrogenase complex structure and function.

PubMed: 33567276
DOI: 10.1016/j.celrep.2021.108727

実験手法

ELECTRON MICROSCOPY (6.9 Å)