3R3Q

Crystal structure of the yeast Vps23 UEV domain

3R3Q の概要

• エントリーDOI: 10.2210/pdb3r3q/pdb
• 関連するPDBエントリー: 3R42
• 分子名称: Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: endosomal sorting, escrt-i, protein transport
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Cytoplasm: P25604
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19353.44

構造登録者

Ren, X.,Hurley, J.H. (登録日: 2011-03-16, 公開日: 2011-05-04, 最終更新日: 2023-09-13)

主引用文献

Ren, X.,Hurley, J.H.
Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast.
Embo J., 30:2130-2139, 2011

PubMed Abstract: The ESCRT-0 and ESCRT-I complexes coordinate the clustering of ubiquitinated cargo with intralumenal budding of the endosomal membrane, two essential steps in vacuolar/lysosomal protein sorting from yeast to humans. The 1.85-Å crystal structure of interacting regions of the yeast ESCRT-0 and ESCRT-I complexes reveals that PSDP motifs of the Vps27 ESCRT-0 subunit bind to a novel electropositive N-terminal site on the UEV domain of the ESCRT-I subunit Vps23 centred on Trp16. This novel site is completely different from the C-terminal part of the human UEV domain that binds to P(S/T)AP motifs of human ESCRT-0 and HIV-1 Gag. Disruption of the novel PSDP-binding site eliminates the interaction in vitro and blocks enrichment of Vps23 in endosome-related class E compartments in yeast cells. However, this site is non-essential for sorting of the ESCRT cargo Cps1. Taken together, these results show how a conserved motif/domain pair can evolve to use strikingly different binding modes in different organisms.

PubMed: 21505419
DOI: 10.1038/emboj.2011.122

実験手法

X-RAY DIFFRACTION (1.45 Å)