title: Structural and functional insight into the N-terminal domain of the clathrin adaptor Ent5 from Saccharomyces cerevisiae.
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.
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signaling Network, School of Life Science, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China; Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors.forename: Fan
authors.initials: F
authors.lastname: Zhang
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signaling Network, School of Life Science, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China; Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors.forename: Yang
authors.initials: Y
authors.lastname: Song
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signaling Network, School of Life Science, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China; Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors.forename: Mohammad
authors.initials: M
authors.lastname: Ebrahimi
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signaling Network, School of Life Science, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China; Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors.forename: Liwen
authors.initials: L
authors.lastname: Niu
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signaling Network, School of Life Science, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China; Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China. Electronic address: mkteng@ustc.edu.cn.
authors.forename: Maikun
authors.initials: M
authors.lastname: Teng
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signaling Network, School of Life Science, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China; Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China. Electronic address: sachem@ustc.edu.cn.
authors.forename: Xu
authors.initials: X
authors.lastname: Li
mesh_terms: D033942:Adaptor Proteins, Vesicular Transport / Q000737:chemistry / Q000235:genetics* / Q000648:ultrastructure*; D019143:Evolution, Molecular; D011487:Protein Conformation; D000072417:Protein Domains; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics* / Q000648:ultrastructure*; D013329:Structure-Activity Relationship
chemical_list: D033942:Adaptor Proteins, Vesicular Transport; C495588:Ent5 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins
keywords: Classification; Clathrin-coated vesicle; Crystal structure; Phosphoinositide; Saccharomyces cerevisiae; ScEnt5