5J08

Crystal structure of yeast Ent5 N-terminal domain-native P21

5J08 の概要

• エントリーDOI: 10.2210/pdb5j08/pdb
• 分子名称: Epsin-5 (2 entities in total)
• 機能のキーワード: vesicular transport, ent5, n-terminal domain, inositol phosphate, protein transport
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
• 細胞内の位置: Cytoplasm: Q03769
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20277.49

構造登録者

Zhang, F.,Song, Y.,Li, X.,Teng, M.K. (登録日: 2016-03-28, 公開日: 2016-10-05, 最終更新日: 2023-11-08)

主引用文献

Zhang, F.,Song, Y.,Ebrahimi, M.,Niu, L.,Teng, M.K.,Li, X.
Structural and functional insight into the N-terminal domain of the clathrin adaptor Ent5 from Saccharomyces cerevisiae
Biochem.Biophys.Res.Commun., 477:786-793, 2016

PubMed Abstract: Clathrin-coated vesicles (CCVs) play critical roles in multiple cellular processes, including nutrient uptake, endosome/lysosome biogenesis, pathogen invasion, regulation of signalling receptors, etc. Saccharomyces cerevisiae Ent5 (ScEnt5) is one of the two major adaptors supporting the CCV-mediated TGN/endosome traffic in yeast cells. However, the classification and phosphoinositide binding characteristic of ScEnt5 remain elusive. Here we report the crystal structures of the ScEnt5 N-terminal domain, and find that ScEnt5 contains an insertion α' helix that does not exist in other ENTH or ANTH domains. Furthermore, we investigate the classification of ScEnt5-N(31-191) by evolutionary history analyses and structure comparisons, and find that the ScEnt5 N-terminal domain shows different phosphoinositide binding property from rEpsin1 and rCALM. Above results facilitate the understanding of the ScEnt5-mediated vesicle coat formation process.

PubMed: 27369074
DOI: 10.1016/j.bbrc.2016.06.136

実験手法

X-RAY DIFFRACTION (1.8 Å)