3DYU

Crystal structure of Snx9PX-BAR (230-595), H32

Summary for 3DYU

• Entry DOI: 10.2210/pdb3dyu/pdb
• Related: 3DYT
• Descriptor: Sorting nexin-9 (1 entity in total)
• Functional Keywords: 3-helix-bundle, bar domain, px domain, phosphoprotein, protein transport, sh3 domain, transport, transport protein
• Biological source: Homo sapiens
• Cellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: Q9Y5X1
• Total number of polymer chains: 3
• Total formula weight: 127273.83

Authors

Wang, Q.,Kaan, H.Y.K.,Sondermann, H. (deposition date: 2008-07-28, release date: 2008-09-16, Last modification date: 2023-08-30)

Primary citation

Wang, 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

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

Experimental method

X-RAY DIFFRACTION (4.1 Å)