5CB2
the structure of candida albicans Sey1p in complex with GMPPNP
Summary for 5CB2
| Entry DOI | 10.2210/pdb5cb2/pdb |
| Related | 5CA8 5CA9 |
| Descriptor | Protein SEY1, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | er, membrance fusion, dynamin, sey1p, hydrolase |
| Biological source | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Cellular location | Endoplasmic reticulum membrane ; Multi-pass membrane protein : Q9C0L9 |
| Total number of polymer chains | 1 |
| Total formula weight | 79670.50 |
| Authors | |
| Primary citation | 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 Cited by 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: 26370501DOI: 10.1083/jcb.201502078 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
