6SH4

Structure of the Apo1 state of the heptameric Bcs1 AAA-ATPase.

6SH4 の概要

• エントリーDOI: 10.2210/pdb6sh4/pdb
• EMDBエントリー: 10192 10193
• 分子名称: Mitochondrial chaperone BCS1 (1 entity in total)
• 機能のキーワード: translocation, rieske, mitochondira, inner mitochondiral membrane, translocase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 358206.35

構造登録者

Kater, L.,Beckmann, R. (登録日: 2019-08-05, 公開日: 2020-02-05, 最終更新日: 2024-05-22)

主引用文献

Kater, L.,Wagener, N.,Berninghausen, O.,Becker, T.,Neupert, W.,Beckmann, R.
Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins.
Nat.Struct.Mol.Biol., 27:142-149, 2020

PubMed Abstract: Some proteins require completion of folding before translocation across a membrane into another cellular compartment. Yet the permeability barrier of the membrane should not be compromised and mechanisms have remained mostly elusive. Here, we present the structure of Saccharomyces cerevisiae Bcs1, an AAA-ATPase of the inner mitochondrial membrane. Bcs1 facilitates the translocation of the Rieske protein, Rip1, which requires folding and incorporation of a 2Fe-2S cluster before translocation and subsequent integration into the bc1 complex. Surprisingly, Bcs1 assembles into exclusively heptameric homo-oligomers, with each protomer consisting of an amphipathic transmembrane helix, a middle domain and an ATPase domain. Together they form two aqueous vestibules, the first being accessible from the mitochondrial matrix and the second positioned in the inner membrane, with both separated by the seal-forming middle domain. On the basis of this unique architecture, we propose an airlock-like translocation mechanism for folded Rip1.

PubMed: 31988523
DOI: 10.1038/s41594-019-0364-1

実験手法

ELECTRON MICROSCOPY (4.4 Å)