6D80

Cryo-EM structure of the mitochondrial calcium uniporter from N. fischeri bound to saposin

6D80 の概要

• エントリーDOI: 10.2210/pdb6d80/pdb
• 関連するPDBエントリー: 6D7W
• EMDBエントリー: 7826 7828
• 分子名称: Saposin A, Mitochondrial calcium uniporter, CALCIUM ION (3 entities in total)
• 機能のキーワード: mitochondria, calcium channel, transport protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 233221.16

構造登録者

Nguyen, N.X.,Armache, J.-P.,Cheng, Y.,Bai, X.C. (登録日: 2018-04-25, 公開日: 2018-07-11, 最終更新日: 2024-05-15)

主引用文献

Nguyen, N.X.,Armache, J.-P.,Lee, C.,Yang, Y.,Zeng, W.,Mootha, V.K.,Cheng, Y.,Bai, X.C.,Jiang, Y.
Cryo-EM structure of a fungal mitochondrial calcium uniporter.
Nature, 559:570-574, 2018

PubMed Abstract: The mitochondrial calcium uniporter (MCU) is a highly selective calcium channel localized to the inner mitochondrial membrane. Here, we describe the structure of an MCU orthologue from the fungus Neosartorya fischeri (NfMCU) determined to 3.8 Å resolution by phase-plate cryo-electron microscopy. The channel is a homotetramer with two-fold symmetry in its amino-terminal domain (NTD) that adopts a similar structure to that of human MCU. The NTD assembles as a dimer of dimers to form a tetrameric ring that connects to the transmembrane domain through an elongated coiled-coil domain. The ion-conducting pore domain maintains four-fold symmetry, with the selectivity filter positioned at the start of the pore-forming TM2 helix. The aspartate and glutamate sidechains of the conserved DIME motif are oriented towards the central axis and separated by one helical turn. The structure of NfMCU offers insights into channel assembly, selective calcium permeation, and inhibitor binding.

PubMed: 29995855
DOI: 10.1038/s41586-018-0333-6

実験手法

ELECTRON MICROSCOPY (5 Å)