7PRO

Structure of CtAtm1 in the inward-open with Glutathione-complexed [2Fe-2S] cluster bound

7PRO の概要

• エントリーDOI: 10.2210/pdb7pro/pdb
• EMDBエントリー: 13606 13607 13609
• 分子名称: Putative iron-sulfur protein (1 entity in total)
• 機能のキーワード: abc exporter, membrane protein
• 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: 2
• 化学式量合計: 154399.62

構造登録者

Li, P.,Wang, K.T.,Gourdon, P.E. (登録日: 2021-09-22, 公開日: 2022-08-10, 最終更新日: 2024-07-17)

主引用文献

Li, P.,Hendricks, A.L.,Wang, Y.,Villones, R.L.E.,Lindkvist-Petersson, K.,Meloni, G.,Cowan, J.A.,Wang, K.,Gourdon, P.
Structures of Atm1 provide insight into [2Fe-2S] cluster export from mitochondria.
Nat Commun, 13:4339-4339, 2022

PubMed Abstract: In eukaryotes, iron-sulfur clusters are essential cofactors for numerous physiological processes, but these clusters are primarily biosynthesized in mitochondria. Previous studies suggest mitochondrial ABCB7-type exporters are involved in maturation of cytosolic iron-sulfur proteins. However, the molecular mechanism for how the ABCB7-type exporters participate in this process remains elusive. Here, we report a series of cryo-electron microscopy structures of a eukaryotic homolog of human ABCB7, CtAtm1, determined at average resolutions ranging from 2.8 to 3.2 Å, complemented by functional characterization and molecular docking in silico. We propose that CtAtm1 accepts delivery from glutathione-complexed iron-sulfur clusters. A partially occluded state links cargo-binding to residues at the mitochondrial matrix interface that line a positively charged cavity, while the binding region becomes internalized and is partially divided in an early occluded state. Collectively, our findings substantially increase the understanding of the transport mechanism of eukaryotic ABCB7-type proteins.

PubMed: 35896548
DOI: 10.1038/s41467-022-32006-8

実験手法

ELECTRON MICROSCOPY (3 Å)