5H3D

Helical structure of membrane tubules decorated by ACAP1 (BARPH doamin) protein by cryo-electron microscopy and MD simulation

5H3D の概要

• エントリーDOI: 10.2210/pdb5h3d/pdb
• EMDBエントリー: 2546
• 分子名称: Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 (1 entity in total)
• 機能のキーワード: acap1 barph domain, membrane remodeling, molecular dynamics simulation, signaling 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: 173337.39

構造登録者

Chan, C.,Pang, X.Y.,Zhang, Y.,Sun, F.,Fan, J. (登録日: 2016-10-22, 公開日: 2019-01-16, 最終更新日: 2024-03-20)

主引用文献

Chan, C.,Pang, X.,Zhang, Y.,Niu, T.,Yang, S.,Zhao, D.,Li, J.,Lu, L.,Hsu, V.W.,Zhou, J.,Sun, F.,Fan, J.
ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages.
Plos Comput.Biol., 15:e1007081-e1007081, 2019

PubMed Abstract: Studies on the Bin-Amphiphysin-Rvs (BAR) domain have advanced a fundamental understanding of how proteins deform membrane. We previously showed that a BAR domain in tandem with a Pleckstrin Homology (PH domain) underlies the assembly of ACAP1 (Arfgap with Coil-coil, Ankryin repeat, and PH domain I) into an unusual lattice structure that also uncovers a new paradigm for how a BAR protein deforms membrane. Here, we initially pursued computation-based refinement of the ACAP1 lattice to identify its critical protein contacts. Simulation studies then revealed how ACAP1, which dimerizes into a symmetrical structure in solution, is recruited asymmetrically to the membrane through dynamic behavior. We also pursued electron microscopy (EM)-based structural studies, which shed further insight into the dynamic nature of the ACAP1 lattice assembly. As ACAP1 is an unconventional BAR protein, our findings broaden the understanding of the mechanistic spectrum by which proteins assemble into higher-ordered structures to achieve membrane deformation.

PubMed: 31291238
DOI: 10.1371/journal.pcbi.1007081

実験手法

ELECTRON MICROSCOPY (14 Å)