6UKS

ATPgammaS bound mBcs1

6UKS の概要

• エントリーDOI: 10.2210/pdb6uks/pdb
• EMDBエントリー: 20811
• 分子名称: Mitochondrial chaperone BCS1, MAGNESIUM ION, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER (3 entities in total)
• 機能のキーワード: bcs1, aaa atpases, mitochondrial inner membrane, chaperone
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 344447.83

構造登録者

Tang, W.K.,Borgnia, M.J.,Hsu, A.L.,Xia, D. (登録日: 2019-10-05, 公開日: 2020-02-05, 最終更新日: 2020-02-26)

主引用文献

Tang, W.K.,Borgnia, M.J.,Hsu, A.L.,Esser, L.,Fox, T.,de Val, N.,Xia, D.
Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein.
Nat.Struct.Mol.Biol., 27:202-209, 2020

PubMed Abstract: The mitochondrial membrane-bound AAA protein Bcs1 translocate substrates across the mitochondrial inner membrane without previous unfolding. One substrate of Bcs1 is the iron-sulfur protein (ISP), a subunit of the respiratory Complex III. How Bcs1 translocates ISP across the membrane is unknown. Here we report structures of mouse Bcs1 in two different conformations, representing three nucleotide states. The apo and ADP-bound structures reveal a homo-heptamer and show a large putative substrate-binding cavity accessible to the matrix space. ATP binding drives a contraction of the cavity by concerted motion of the ATPase domains, which could push substrate across the membrane. Our findings shed light on the potential mechanism of translocating folded proteins across a membrane, offer insights into the assembly process of Complex III and allow mapping of human disease-associated mutations onto the Bcs1 structure.

PubMed: 32042153
DOI: 10.1038/s41594-020-0373-0

実験手法

ELECTRON MICROSCOPY (3.2 Å)