1FIO

CRYSTAL STRUCTURE OF YEAST T-SNARE PROTEIN SSO1

1FIO の概要

• エントリーDOI: 10.2210/pdb1fio/pdb
• 分子名称: SSO1 PROTEIN, ZINC ION (3 entities in total)
• 機能のキーワード: four helix bundle, alpha helix, membrane protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Membrane; Single-pass type IV membrane protein (Potential): P32867
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22929.24

構造登録者

Munson, M.,Chen, X.,Cocina, A.E.,Schultz, S.M.,Hughson, F.M. (登録日: 2000-08-04, 公開日: 2000-10-11, 最終更新日: 2024-05-22)

主引用文献

Munson, M.,Chen, X.,Cocina, A.E.,Schultz, S.M.,Hughson, F.M.
Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly.
Nat.Struct.Biol., 7:894-902, 2000

PubMed Abstract: In the eukaryotic secretory and endocytic pathways, transport vesicles shuttle cargo among intracellular organelles and to and from the plasma membrane. Cargo delivery entails fusion of the transport vesicle with its target, a process thought to be mediated by membrane bridging SNARE protein complexes. Temporal and spatial control of intracellular trafficking depends in part on regulating the assembly of these complexes. In vitro, SNARE assembly is inhibited by the closed conformation adopted by the syntaxin family of SNAREs. To visualize this closed conformation directly, the X-ray crystal structure of a yeast syntaxin, Sso1p, has been determined and refined to 2.1 A resolution. Mutants designed to destabilize the closed conformation exhibit accelerated rates of SNARE assembly. Our results provide insight into the mechanism of SNARE assembly and its intramolecular and intermolecular regulation.

PubMed: 11017200
DOI: 10.1038/79659

実験手法

X-RAY DIFFRACTION (2.1 Å)