2OAJ

Crystal structure of Sro7 from S. cerevisiae

2OAJ の概要

• エントリーDOI: 10.2210/pdb2oaj/pdb
• 分子名称: Protein SNI1, ZINC ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: wd40 repeat, beta propeller, endocytosis-exocytosis complex, endocytosis/exocytosis
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: Q12038
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 100225.58

構造登録者

Hattendorf, D.A.,Weis, W.I. (登録日: 2006-12-15, 公開日: 2007-04-03, 最終更新日: 2023-12-27)

主引用文献

Hattendorf, D.A.,Andreeva, A.,Gangar, A.,Brennwald, P.J.,Weis, W.I.
Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism.
Nature, 446:567-571, 2007

PubMed Abstract: Polarized exocytosis requires coordination between the actin cytoskeleton and the exocytic machinery responsible for fusion of secretory vesicles at specific sites on the plasma membrane. Fusion requires formation of a complex between a vesicle-bound R-SNARE and plasma membrane Qa, Qb and Qc SNARE proteins. Proteins in the lethal giant larvae protein family, including lethal giant larvae and tomosyn in metazoans and Sro7 in yeast, interact with Q-SNAREs and are emerging as key regulators of polarized exocytosis. The crystal structure of Sro7 reveals two seven-bladed WD40 beta-propellers followed by a 60-residue-long 'tail', which is bound to the surface of the amino-terminal propeller. Deletion of the Sro7 tail enables binding to the Qbc SNARE region of Sec9 and this interaction inhibits SNARE complex assembly. The N-terminal domain of Sec9 provides a second, high-affinity Sro7 interaction that is unaffected by the tail. The results suggest that Sro7 acts as an allosteric regulator of exocytosis through interactions with factors that control the tail. Sequence alignments indicate that lethal giant larvae and tomosyn have a two-beta-propeller fold similar to that of Sro7, but only tomosyn appears to retain the regulatory tail.

PubMed: 17392788
DOI: 10.1038/nature05635

実験手法

X-RAY DIFFRACTION (2.4 Å)