3GRL

Crystal Structure of the Monomer of the p115 Tether Globular Head Domain

3GRL の概要

• エントリーDOI: 10.2210/pdb3grl/pdb
• 関連するPDBエントリー: 3gq2
• 分子名称: General vesicular transport factor p115, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: vesicle transport, membrane trafficking, membrane tethering, membrane fusion, snare, rab gtpase, armadillo repeats, er-golgi transport, golgi apparatus, membrane, phosphoprotein, protein transport, transport, transport protein
• 由来する生物種: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• 細胞内の位置: Cytoplasm, cytosol: P41541
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 72761.96

構造登録者

An, Y.,Elsliger, M.A.,Wilson, I.A. (登録日: 2009-03-25, 公開日: 2009-11-03, 最終更新日: 2024-02-21)

主引用文献

An, Y.,Chen, C.Y.,Moyer, B.,Rotkiewicz, P.,Elsliger, M.A.,Godzik, A.,Wilson, I.A.,Balch, W.E.
Structural and functional analysis of the globular head domain of p115 provides insight into membrane tethering.
J.Mol.Biol., 391:26-41, 2009

PubMed Abstract: Molecular tethers have a central role in the organization of the complex membrane architecture of eukaryotic cells. p115 is a ubiquitous, essential tether involved in vesicle transport and the structural organization of the exocytic pathway. We describe two crystal structures of the N-terminal domain of p115 at 2.0 A resolution. The p115 structures show a novel alpha-solenoid architecture constructed of 12 armadillo-like, tether-repeat, alpha-helical tripod motifs. We find that the H1 TR binds the Rab1 GTPase involved in endoplasmic reticulum to Golgi transport. Mutation of the H1 motif results in the dominant negative inhibition of endoplasmic reticulum to Golgi trafficking. We propose that the H1 helical tripod contributes to the assembly of Rab-dependent complexes responsible for the tether and SNARE-dependent fusion of membranes.

PubMed: 19414022
DOI: 10.1016/j.jmb.2009.04.062

実験手法

X-RAY DIFFRACTION (2 Å)