5CMW

Crystal structure of yeast Ent5 N-terminal domain-soaked in KI

Summary for 5CMW

• Entry DOI: 10.2210/pdb5cmw/pdb
• Related: 5CMY
• Descriptor: Epsin-5, GLYCEROL, IODIDE ION, ... (4 entities in total)
• Functional Keywords: vesicular transport, ent5, n-terminal domain, inositol phosphate, protein transport
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Yeast)
• Cellular location: Cytoplasm: Q03769
• Total number of polymer chains: 1
• Total formula weight: 22146.24

Authors

Zhang, F.,Song, Y.,Li, X.,Teng, M.K. (deposition date: 2015-07-17, release date: 2016-07-20, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)