6DNF

Cryo-EM structure of the mitochondrial calcium uniporter MCU from the fungus Cyphellophora europaea

6DNF の概要

• エントリーDOI: 10.2210/pdb6dnf/pdb
• EMDBエントリー: 7971 7972
• 分子名称: Mitochondrial calcium uniporter MCU, 1-[GLYCEROLYLPHOSPHONYL]-2-[8-(2-HEXYL-CYCLOPROPYL)-OCTANAL-1-YL]-3-[HEXADECANAL-1-YL]-GLYCEROL, CALCIUM ION (3 entities in total)
• 機能のキーワード: mitochondria, calcium, ion channel, eukaryotic, membrane protein
• 由来する生物種: Cyphellophora europaea CBS 101466
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 164548.79

構造登録者

Long, S.B.,Baradaran, R.,Wang, C. (登録日: 2018-06-06, 公開日: 2018-07-11, 最終更新日: 2024-03-13)

主引用文献

Baradaran, R.,Wang, C.,Siliciano, A.F.,Long, S.B.
Cryo-EM structures of fungal and metazoan mitochondrial calcium uniporters.
Nature, 559:580-584, 2018

PubMed Abstract: The mitochondrial calcium uniporter (MCU) is a highly selective calcium channel and a major route of calcium entry into mitochondria. How the channel catalyses ion permeation and achieves ion selectivity are not well understood, partly because MCU is thought to have a distinct architecture in comparison to other cellular channels. Here we report cryo-electron microscopy reconstructions of MCU channels from zebrafish and Cyphellophora europaea at 8.5 Å and 3.2 Å resolutions, respectively. In contrast to a previous report of pentameric stoichiometry for MCU, both channels are tetramers. The atomic model of C. europaea MCU shows that a conserved WDXXEP signature sequence forms the selectivity filter, in which calcium ions are arranged in single file. Coiled-coil legs connect the pore to N-terminal domains in the mitochondrial matrix. In C. europaea MCU, the N-terminal domains assemble as a dimer of dimers; in zebrafish MCU, they form an asymmetric crescent. The structures define principles that underlie ion permeation and calcium selectivity in this unusual channel.

PubMed: 29995857
DOI: 10.1038/s41586-018-0331-8

実験手法

ELECTRON MICROSCOPY (3.2 Å)