6WUM

Mitochondrial SAM complex - dimer 2 in detergent

6WUM の概要

• エントリーDOI: 10.2210/pdb6wum/pdb
• EMDBエントリー: 21913 21914 21915 21916 21917
• 分子名称: Sam35, Tom37 domain-containing protein, Bac_surface_Ag domain-containing protein (3 entities in total)
• 機能のキーワード: mitochondrial sam complex, sam35, sam37, sam50., membrane protein
• 由来する生物種: Thermothelomyces thermophilus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 278976.32

構造登録者

Ni, X.,Botos, I.,Diederichs, K. (登録日: 2020-05-04, 公開日: 2020-08-12, 最終更新日: 2024-03-06)

主引用文献

Diederichs, K.A.,Ni, X.,Rollauer, S.E.,Botos, I.,Tan, X.,King, M.S.,Kunji, E.R.S.,Jiang, J.,Buchanan, S.K.
Structural insight into mitochondrial beta-barrel outer membrane protein biogenesis.
Nat Commun, 11:3290-3290, 2020

PubMed Abstract: In mitochondria, β-barrel outer membrane proteins mediate protein import, metabolite transport, lipid transport, and biogenesis. The Sorting and Assembly Machinery (SAM) complex consists of three proteins that assemble as a 1:1:1 complex to fold β-barrel proteins and insert them into the mitochondrial outer membrane. We report cryoEM structures of the SAM complex from Myceliophthora thermophila, which show that Sam50 forms a 16-stranded transmembrane β-barrel with a single polypeptide-transport-associated (POTRA) domain extending into the intermembrane space. Sam35 and Sam37 are located on the cytosolic side of the outer membrane, with Sam35 capping Sam50, and Sam37 interacting extensively with Sam35. Sam35 and Sam37 each adopt a GST-like fold, with no functional, structural, or sequence similarity to their bacterial counterparts. Structural analysis shows how the Sam50 β-barrel opens a lateral gate to accommodate its substrates.

PubMed: 32620929
DOI: 10.1038/s41467-020-17144-1

実験手法

ELECTRON MICROSCOPY (3.6 Å)