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DOI | 10.2210/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: 29899447DOI: 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) |
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