8V8T

Asymmetrical subunit from a Drp1 lattice on PA nanotubes

これはPDB形式変換不可エントリーです。

8V8T の概要

• エントリーDOI: 10.2210/pdb8v8t/pdb
• EMDBエントリー: 43045
• 分子名称: Dynamin-1-like protein (1 entity in total)
• 機能のキーワード: membrane remodeling gtpase, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 330435.16

構造登録者

Rochon, K.,Peng, R.,Hutson, A.N.,Stagg, S.M.,Mears, J.A. (登録日: 2023-12-06, 公開日: 2025-04-16, 最終更新日: 2025-04-30)

主引用文献

Peng, R.,Rochon, K.,Hutson, A.N.,Stagg, S.M.,Mears, J.A.
The Structure of the Drp1 Lattice on Membrane.
J.Mol.Biol., 437:169125-169125, 2025

PubMed Abstract: Mitochondrial health relies on the membrane fission mediated by dynamin-related protein 1 (Drp1). Previous structural studies of Drp1 on remodeled membranes were hampered by heterogeneity, leaving a critical gap in the understanding of the mitochondrial fission mechanisms. Here we present a cryo-electron microscopy structure of full-length human Drp1 decorated on membrane tubules. Using the reconstruction of average subtracted tubular regions (RASTR) technique, we report that Drp1 forms a locally ordered lattice along the tubule without global helical symmetry. The filaments in the lattice are similar to dynamin rungs with conserved stalk interactions. Adjacent filaments are connected by GTPase domain interactions in a novel stacked conformation. We identified two states of the Drp1 lattice among the heterogenous dataset representing conformational changes around hinge 1. Additionally, we observed contact between Drp1 and membrane that can be assigned to the variable domain sequence. Together these structures revealed a putative mechanism by which Drp1 constricts mitochondria membranes in a stepwise, "ratchet" manner.

PubMed: 40185198
DOI: 10.1016/j.jmb.2025.169125

実験手法

ELECTRON MICROSCOPY (14.73 Å)