2RAJ
SO4 bound PX-BAR membrane remodeling unit of Sorting Nexin 9
Summary for 2RAJ
Entry DOI | 10.2210/pdb2raj/pdb |
Related | 2RAI 2RAK |
Descriptor | Sorting nexin-9, SULFATE ION (3 entities in total) |
Functional Keywords | sorting nexin, membrane transport, px domain, bar domain, tubulation, structural protein |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: Q9Y5X1 |
Total number of polymer chains | 1 |
Total formula weight | 45393.09 |
Authors | Pylypenko, O.,Lundmark, R.,Rasmuson, E.,Carlsson, S.R.,Rak, A. (deposition date: 2007-09-16, release date: 2007-12-11, Last modification date: 2024-02-21) |
Primary citation | Pylypenko, O.,Lundmark, R.,Rasmuson, E.,Carlsson, S.R.,Rak, A. The PX-BAR membrane-remodeling unit of sorting nexin 9 Embo J., 26:4788-4800, 2007 Cited by PubMed Abstract: Sorting nexins (SNXs) form a family of proteins known to interact with components in the endosomal system and to regulate various steps of vesicle transport. Sorting nexin 9 (SNX9) is involved in the late stages of clathrin-mediated endocytosis in non-neuronal cells, where together with the GTPase dynamin, it participates in the formation and scission of the vesicle neck. We report here crystal structures of the functional membrane-remodeling unit of SNX9 and show that it efficiently tubulates lipid membranes in vivo and in vitro. Elucidation of the protein superdomain structure, together with mutational analysis and biochemical and cell biological experiments, demonstrated how the SNX9 PX and BAR domains work in concert in targeting and tubulation of phosphoinositide-containing membranes. The study provides insights into the SNX9-induced membrane modulation mechanism. PubMed: 17948057DOI: 10.1038/sj.emboj.7601889 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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