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2RAJ

SO4 bound PX-BAR membrane remodeling unit of Sorting Nexin 9

Summary for 2RAJ
Entry DOI10.2210/pdb2raj/pdb
Related2RAI 2RAK
DescriptorSorting nexin-9, SULFATE ION (3 entities in total)
Functional Keywordssorting nexin, membrane transport, px domain, bar domain, tubulation, structural protein
Biological sourceHomo sapiens (human)
Cellular locationCytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: Q9Y5X1
Total number of polymer chains1
Total formula weight45393.09
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 citationPylypenko, 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: 17948057
DOI: 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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건을2024-11-06부터공개중

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