9JVQ

Yeast Mitochondrial PORIN complex

9JVQ の概要

• エントリーDOI: 10.2210/pdb9jvq/pdb
• EMDBエントリー: 61843
• 分子名称: Non-selective voltage-gated ion channel 1 (1 entity in total)
• 機能のキーワード: transport protein
• 由来する生物種: Saccharomyces cerevisiae S288C
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 182732.26

構造登録者

Takeda, H.,Endo, T.,Kikkawa, M.,Tsutsumi, A. (登録日: 2024-10-09, 公開日: 2025-08-13)

主引用文献

Takeda, H.,Shinoda, S.,Goto, C.,Tsutsumi, A.,Sakaue, H.,Zhang, C.,Hirashima, T.,Konishi, Y.,Ono, H.,Yamamori, Y.,Tomii, K.,Shiino, H.,Tamura, Y.,Zuttion, S.,Senger, B.,Friant, S.,Becker, H.D.,Araiso, Y.,Kobayashi, N.,Kodera, N.,Kikkawa, M.,Endo, T.
Oligomer-based functions of mitochondrial porin.
Nat Commun, 16:6854-6854, 2025

PubMed Abstract: Porin, or the voltage-dependent anion channel (VDAC), is a primary β-barrel channel in the mitochondrial outer membrane. It transports small metabolites and ions through its β-barrel pore and plays key roles in apoptosis and inflammatory response. Here we report the cryo-electron microscopy structure of yeast porin (Por1) in its hexameric form at 3.2 Å resolution. This structure allows us to introduce various mutations at the protomer interfaces, uncovering three critical functions of Por1 assembly beyond transport. Por1 binds unassembled Tom22, a subunit of the mitochondrial protein import gate (the TOM complex), to facilitate protein import into the intermembrane space, maintains proper mitochondrial lipid composition in the outer membrane through lipid scramblase activity, and contributes to the retention and regulated loss of mitochondrial DNA, in cooperation with nucleases identified through screening enabled by the obtained Por1 mutant.

PubMed: 40715117
DOI: 10.1038/s41467-025-62021-4

実験手法

ELECTRON MICROSCOPY (3.2 Å)