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3DYT

Crystal structure of Snx9PX-BAR (230-595), C2221

Summary for 3DYT
Entry DOI10.2210/pdb3dyt/pdb
Related3DYU
DescriptorSorting nexin-9, SULFATE ION (3 entities in total)
Functional Keywords3-helix bundle, bar domain, px domain, phosphoprotein, protein transport, sh3 domain, transport, transport protein
Biological sourceHomo sapiens
Cellular locationCytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: Q9Y5X1
Total number of polymer chains1
Total formula weight43177.20
Authors
Wang, Q.,Kaan, H.Y.K.,Sondermann, H. (deposition date: 2008-07-28, release date: 2008-09-16, Last modification date: 2024-10-30)
Primary citationWang, Q.,Kaan, H.Y.,Hooda, R.N.,Goh, S.L.,Sondermann, H.
Structure and plasticity of endophilin and sorting nexin 9.
Structure, 16:1574-1587, 2008
Cited by
PubMed Abstract: Endophilin and Sorting Nexin 9 (Snx9) play key roles in endocytosis by membrane curvature sensing and remodeling via their Bin/Amphiphysin/Rvs (BAR) domains. BAR and the related F-BAR domains form dimeric, crescent-shaped units that occur N- or C-terminally to other lipid-binding, adaptor, or catalytic modules. In crystal structures, the PX-BAR unit of Snx9 (Snx9(PX-BAR)) adopts an overall compact, moderately curved conformation. SAXS-based solution studies revealed an alternative, more curved state of Snx9(PX-BAR) in which the PX domains are flexibly connected to the BAR domains, providing a model for how Snx9 exhibits lipid-dependent curvature preferences. In contrast, Endophilin appears to be rigid in solution, and the SH3 domains are located at the distal tips of a BAR domain dimer with fixed curvature. We also observed tip-to-tip interactions between the BAR domains in a trigonal crystal form of Snx9(PX-BAR) reminiscent of functionally important interactions described for F-BAR domains.
PubMed: 18940612
DOI: 10.1016/j.str.2008.07.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.08 Å)
Structure validation

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