3NS4

Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of GARP to a family of tethering complexes

3NS4 の概要

• エントリーDOI: 10.2210/pdb3ns4/pdb
• 分子名称: Vacuolar protein sorting-associated protein 53, BARIUM ION (3 entities in total)
• 機能のキーワード: garp complex component, helical bundle, membrane tethering complex, membrane traffic, vps51, vps52, vps54, arl1, protein binding
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: P47061
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32300.33

構造登録者

Vasan, N.,Reinisch, K.M. (登録日: 2010-07-01, 公開日: 2010-09-15, 最終更新日: 2024-10-09)

主引用文献

Vasan, N.,Hutagalung, A.,Novick, P.,Reinisch, K.M.
Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes.
Proc.Natl.Acad.Sci.USA, 107:14176-14181, 2010

PubMed Abstract: The Golgi-associated retrograde protein (GARP) complex is a membrane-tethering complex that functions in traffic from endosomes to the trans-Golgi network. Here we present the structure of a C-terminal fragment of the Vps53 subunit, important for binding endosome-derived vesicles, at a resolution of 2.9 A. We show that the C terminus consists of two alpha-helical bundles arranged in tandem, and we identify a highly conserved surface patch, which may play a role in vesicle recognition. Mutations of the surface result in defects in membrane traffic. The fold of the Vps53 C terminus is strongly reminiscent of proteins that belong to three other tethering complexes--Dsl1, conserved oligomeric Golgi, and the exocyst--thought to share a common evolutionary origin. Thus, the structure of the Vps53 C terminus suggests that GARP belongs to this family of complexes.

PubMed: 20660722
DOI: 10.1073/pnas.1009419107

実験手法

X-RAY DIFFRACTION (2.9 Å)