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5WP9

Structural Basis of Mitochondrial Receptor Binding and Constriction by Dynamin-Related Protein 1

これはPDB形式変換不可エントリーです。
5WP9 の概要
エントリーDOI10.2210/pdb5wp9/pdb
EMDBエントリー8874
分子名称Dynamin-1-like protein, Mitochondrial dynamics protein MID49, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, ... (4 entities in total)
機能のキーワードmitochondrial division, dynamin related-protein-1, nucleotide, mid49, protein fibril
由来する生物種Homo sapiens (Human)
詳細
タンパク質・核酸の鎖数16
化学式量合計929988.29
構造登録者
Kalia, R.,Wang, R.Y.R.,Yusuf, A.,Thomas, P.V.,Agard, D.A.,Shaw, J.M.,Frost, A. (登録日: 2017-08-03, 公開日: 2018-06-20, 最終更新日: 2024-03-13)
主引用文献Kalia, R.,Wang, R.Y.,Yusuf, A.,Thomas, P.V.,Agard, D.A.,Shaw, J.M.,Frost, A.
Structural basis of mitochondrial receptor binding and constriction by DRP1.
Nature, 558:401-405, 2018
Cited by
PubMed Abstract: Mitochondrial inheritance, genome maintenance and metabolic adaptation depend on organelle fission by dynamin-related protein 1 (DRP1) and its mitochondrial receptors. DRP1 receptors include the paralogues mitochondrial dynamics proteins of 49 and 51 kDa (MID49 and MID51) and mitochondrial fission factor (MFF); however, the mechanisms by which these proteins recruit and regulate DRP1 are unknown. Here we present a cryo-electron microscopy structure of full-length human DRP1 co-assembled with MID49 and an analysis of structure- and disease-based mutations. We report that GTP induces a marked elongation and rotation of the GTPase domain, bundle-signalling element and connecting hinge loops of DRP1. In this conformation, a network of multivalent interactions promotes the polymerization of a linear DRP1 filament with MID49 or MID51. After co-assembly, GTP hydrolysis and exchange lead to MID receptor dissociation, filament shortening and curling of DRP1 oligomers into constricted and closed rings. Together, these views of full-length, receptor- and nucleotide-bound conformations reveal how DRP1 performs mechanical work through nucleotide-driven allostery.
PubMed: 29899447
DOI: 10.1038/s41586-018-0211-2
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (4.22 Å)
構造検証レポート
Validation report summary of 5wp9
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-07-08に公開中

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