7E4I

Cryo-EM structure of the yeast mitochondrial SAM-Tom40/Tom5/Tom6 complex at 3.0 angstrom

7E4I の概要

• エントリーDOI: 10.2210/pdb7e4i/pdb
• EMDBエントリー: 30985 30986
• 分子名称: Sorting assembly machinery 50 kDa subunit, Sorting assembly machinery 35 kDa subunit, Sorting assembly machinery 37 kDa subunit, ... (6 entities in total)
• 機能のキーワード: translocase
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 189114.74

構造登録者

Wang, Q.,Guan, Z.Y.,Qi, L.B.,Yan, C.Y.,Yin, P. (登録日: 2021-02-13, 公開日: 2021-09-01, 最終更新日: 2025-07-02)

主引用文献

Wang, Q.,Guan, Z.,Qi, L.,Zhuang, J.,Wang, C.,Hong, S.,Yan, L.,Wu, Y.,Cao, X.,Cao, J.,Yan, J.,Zou, T.,Liu, Z.,Zhang, D.,Yan, C.,Yin, P.
Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex.
Science, 373:1377-1381, 2021

PubMed Abstract: β barrel outer membrane proteins (β-OMPs) play vital roles in mitochondria, chloroplasts, and Gram-negative bacteria. Evolutionarily conserved complexes such as the mitochondrial sorting and assembly machinery (SAM) mediate the assembly of β-OMPs. We investigated the SAM-mediated assembly of the translocase of the outer membrane (TOM) core complex. Cryo–electron microscopy structures of SAM–fully folded Tom40 and the SAM-Tom40/Tom5/Tom6 complexes at ~3-angstrom resolution reveal that Sam37 stabilizes the mature Tom40 mainly through electrostatic interactions, thus facilitating subsequent TOM assembly. These results support the β barrel switching model and provide structural insights into the assembly and release of β barrel complexes.

PubMed: 34446444
DOI: 10.1126/science.abh0704

実験手法

ELECTRON MICROSCOPY (3.05 Å)