6BBP

Model for compact volume of truncated monomeric Cytohesin-3 (Grp1; amino acids 63-399) E161A 6GS Arf6 Q67L fusion protein

6BBP の概要

• エントリーDOI: 10.2210/pdb6bbp/pdb
• EMDBエントリー: 7077 7078
• 分子名称: Cytohesin-3,ADP-ribosylation factor 6, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: guanine nucleotide exchange factor, arf gtpase, fusion protein, inositol 1, 3, 4, 5-tetrakisphosphate, lipid binding protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61340.34

構造登録者

Das, S.,Malaby, A.W.,Lambright, D.G. (登録日: 2017-10-19, 公開日: 2018-01-10, 最終更新日: 2024-11-06)

主引用文献

Malaby, A.W.,Das, S.,Chakravarthy, S.,Irving, T.C.,Bilsel, O.,Lambright, D.G.
Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors.
Structure, 26:106-117.e6, 2018

PubMed Abstract: Membrane dynamic processes including vesicle biogenesis depend on Arf guanosine triphosphatase (GTPase) activation by guanine nucleotide exchange factors (GEFs) containing a catalytic Sec7 domain and a membrane-targeting module such as a pleckstrin homology (PH) domain. The catalytic output of cytohesin family Arf GEFs is controlled by autoinhibitory interactions that impede accessibility of the exchange site in the Sec7 domain. These restraints can be relieved through activator Arf-GTP binding to an allosteric site comprising the PH domain and proximal autoinhibitory elements (Sec7-PH linker and C-terminal helix). Small-angle X-ray scattering and negative-stain electron microscopy were used to investigate the structural organization and conformational dynamics of cytohesin-3 (Grp1) in autoinhibited and active states. The results support a model in which hinge dynamics in the autoinhibited state expose the activator site for Arf-GTP binding, while subsequent C-terminal helix unlatching and repositioning unleash conformational entropy in the Sec7-PH linker to drive exposure of the exchange site.

PubMed: 29276036
DOI: 10.1016/j.str.2017.11.019

実験手法

ELECTRON MICROSCOPY (35 Å)