5CB2

the structure of candida albicans Sey1p in complex with GMPPNP

5CB2 の概要

• エントリーDOI: 10.2210/pdb5cb2/pdb
• 関連するPDBエントリー: 5CA8 5CA9
• 分子名称: Protein SEY1, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: er, membrance fusion, dynamin, sey1p, hydrolase
• 由来する生物種: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
• 細胞内の位置: Endoplasmic reticulum membrane ; Multi-pass membrane protein : Q9C0L9
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 79670.50

構造登録者

Yan, L.,Sun, S.,Wang, W.,Shi, J.,Hu, X.,Wang, S.,Rao, Z.,Hu, J.,Lou, Z. (登録日: 2015-06-30, 公開日: 2015-09-23, 最終更新日: 2024-03-20)

主引用文献

Yan, L.,Sun, S.,Wang, W.,Shi, J.,Hu, X.,Wang, S.,Su, D.,Rao, Z.,Hu, J.,Lou, Z.
Structures of the yeast dynamin-like GTPase Sey1p provide insight into homotypic ER fusion
J.Cell Biol., 210:961-972, 2015

PubMed Abstract: Homotypic membrane fusion of the endoplasmic reticulum is mediated by dynamin-like guanosine triphosphatases (GTPases), which include atlastin (ATL) in metazoans and Sey1p in yeast. In this paper, we determined the crystal structures of the cytosolic domain of Sey1p derived from Candida albicans. The structures reveal a stalk-like, helical bundle domain following the GTPase, which represents a previously unidentified configuration of the dynamin superfamily. This domain is significantly longer than that of ATL and critical for fusion. Sey1p forms a side-by-side dimer in complex with GMP-PNP or GDP/AlF4(-) but is monomeric with GDP. Surprisingly, Sey1p could mediate fusion without GTP hydrolysis, even though fusion was much more efficient with GTP. Sey1p was able to replace ATL in mammalian cells, and the punctate localization of Sey1p was dependent on its GTPase activity. Despite the common function of fusogenic GTPases, our results reveal unique features of Sey1p.

PubMed: 26370501
DOI: 10.1083/jcb.201502078

実験手法

X-RAY DIFFRACTION (2.9 Å)