7XRD

Cryo-EM structure of Arf6 helical polymer assembled on lipid membrane

7XRD の概要

• エントリーDOI: 10.2210/pdb7xrd/pdb
• EMDBエントリー: 33414
• 分子名称: ADP-ribosylation factor 6, MAGNESIUM ION, GUANOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: small gtpase, helical polymer, membrane tubulation, lipid binding protein
• 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: 86390.42

構造登録者

Pang, X.Y.,Zhang, Y.,Sun, F. (登録日: 2022-05-10, 公開日: 2023-11-15, 最終更新日: 2025-05-28)

主引用文献

Pang, X.,Zhang, Y.,Park, K.,Liao, Z.,Li, J.,Xu, J.,Hong, M.T.,Yin, G.,Zhang, T.,Wang, Y.,Egelman, E.H.,Fan, J.,Hsu, V.W.,Park, S.Y.,Sun, F.
Structural elucidation of how ARF small GTPases induce membrane tubulation for vesicle fission.
Proc.Natl.Acad.Sci.USA, 122:e2417820122-e2417820122, 2025

PubMed Abstract: ADP-Ribosylation Factor (ARF) small GTPases have been found to act in vesicle fission through a direct ability to tubulate membrane. We have pursued cryoelectron microscopy (EM) to reveal at 3.9 Å resolution how ARF6 assembles into a protein lattice on tubulated membrane. Molecular dynamics simulation studies confirm and extend the cryo-EM findings. The ARF6 lattice exhibits features that are distinct from those formed by other membrane-bending proteins. We identify protein contacts critical for lattice assembly and how membrane insertion results in constricted tubules. The lattice structure also enables docking by GTPase-activating proteins (GAP) to achieve vesiculation. We have also modeled ARF1 onto the ARF6 lattice, and then pursued vesicle reconstitution by the Coat Protein I (COPI) complex to further confirm that the ARF lattice acts in vesicle fission. By elucidating how an ARF protein tubulates membrane at the structural level, we have advanced the molecular understanding of how this class of transport factors promote the fission stage of vesicle formation.

PubMed: 40117306
DOI: 10.1073/pnas.2417820122

実験手法

ELECTRON MICROSCOPY (3.9 Å)