7UOM

Endogenous dihydrolipoamide acetyltransferase (E2) core of pyruvate dehydrogenase complex from bovine kidney

これはPDB形式変換不可エントリーです。

7UOM の概要

• エントリーDOI: 10.2210/pdb7uom/pdb
• EMDBエントリー: 26650
• 分子名称: Acetyltransferase component of pyruvate dehydrogenase complex (1 entity in total)
• 機能のキーワード: e2, pyruvate, dehydrogenase, complex, transferase
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 60
• 化学式量合計: 4148555.64

構造登録者

Liu, S.,Xia, X.,Zhen, J.,Li, Z.H.,Zhou, Z.H. (登録日: 2022-04-13, 公開日: 2022-11-30, 最終更新日: 2024-06-12)

主引用文献

Liu, S.,Xia, X.,Zhen, J.,Li, Z.,Zhou, Z.H.
Structures and comparison of endogenous 2-oxoglutarate and pyruvate dehydrogenase complexes from bovine kidney.
Cell Discov, 8:126-126, 2022

PubMed Abstract: The α-keto acid dehydrogenase complex family catalyzes the essential oxidative decarboxylation of α-keto acids to yield acyl-CoA and NADH. Despite performing the same overarching reaction, members of the family have different component structures and structural organization between each other and across phylogenetic species. While native structures of α-keto acid dehydrogenase complexes from bacteria and fungi became available recently, the atomic structure and organization of their mammalian counterparts in native states remain unknown. Here, we report the cryo-electron microscopy structures of the endogenous cubic 2-oxoglutarate dehydrogenase complex (OGDC) and icosahedral pyruvate dehydrogenase complex (PDC) cores from bovine kidney determined at resolutions of 3.5 Å and 3.8 Å, respectively. The structures of multiple proteins were reconstructed from a single lysate sample, allowing direct structural comparison without the concerns of differences arising from sample preparation and structure determination. Although native and recombinant E2 core scaffold structures are similar, the native structures are decorated with their peripheral E1 and E3 subunits. Asymmetric sub-particle reconstructions support heterogeneity in the arrangements of these peripheral subunits. In addition, despite sharing a similar monomeric fold, OGDC and PDC E2 cores have distinct interdomain and intertrimer interactions, which suggests a means of modulating self-assembly to mitigate heterologous binding between mismatched E2 species. The lipoyl moiety lies near a mobile gatekeeper within the interdomain active site of OGDC E2 and PDC E2. Analysis of the twofold related intertrimer interface identified secondary structural differences and chemical interactions between icosahedral and cubic geometries of the core. Taken together, our study provides a direct structural comparison of OGDC and PDC from the same source and offers new insights into determinants of interdomain interactions and of architecture diversity among α-keto acid dehydrogenase complexes.

PubMed: 36414632
DOI: 10.1038/s41421-022-00487-y

実験手法

ELECTRON MICROSCOPY (3.8 Å)