7Q5Q

Protein community member oxoglutarate dehydrogenase complex E2 core from C. thermophilum

7Q5Q の概要

• エントリーDOI: 10.2210/pdb7q5q/pdb
• EMDBエントリー: 13844
• 分子名称: Dihydrolipoyllysine-residue succinyltransferase (1 entity in total)
• 機能のキーワード: dihydrolipoyl succinyltransferase, e2, oxoglutarate, a-ketoglutarate, transferase
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 1103688.10

構造登録者

Chojnowski, G.,Skalidis, I.,Kyrilis, F.L.,Tueting, C.,Hamdi, F.,Kastritis, P.L. (登録日: 2021-11-04, 公開日: 2022-02-02, 最終更新日: 2023-12-13)

主引用文献

Skalidis, I.,Kyrilis, F.L.,Tuting, C.,Hamdi, F.,Chojnowski, G.,Kastritis, P.L.
Cryo-EM and artificial intelligence visualize endogenous protein community members.
Structure, 30:575-, 2022

PubMed Abstract: Cellular function is underlined by megadalton assemblies organizing in proximity, forming communities. Metabolons are protein communities involving metabolic pathways such as protein, fatty acid, and thioesters of coenzyme-A synthesis. Metabolons are highly heterogeneous due to their function, making their analysis particularly challenging. Here, we simultaneously characterize metabolon-embedded architectures of a 60S pre-ribosome, fatty acid synthase, and pyruvate/oxoglutarate dehydrogenase complex E2 cores de novo. Cryo-electron microscopy (cryo-EM) 3D reconstructions are resolved at 3.84-4.52 Å resolution by collecting <3,000 micrographs of a single cellular fraction. After combining cryo-EM with artificial intelligence-based atomic modeling and de novo sequence identification methods, at this resolution range, polypeptide hydrogen bonding patterns are discernible. Residing molecular components resemble their purified counterparts from other eukaryotes but also exhibit substantial conformational variation with potential functional implications. Our results propose an integrated tool, boosted by machine learning, that opens doors for structural systems biology spearheaded by cryo-EM characterization of native cell extracts.

PubMed: 35093201
DOI: 10.1016/j.str.2022.01.001

実験手法

ELECTRON MICROSCOPY (4.38 Å)