4FVF

SPFH domain of mouse stomatin (Crystal form 1)

Summary for 4FVF

• Entry DOI: 10.2210/pdb4fvf/pdb
• Related: 4FVG 4FVJ
• Descriptor: Stomatin, CADMIUM ION, ACETATE ION, ... (4 entities in total)
• Functional Keywords: mixed alpha-beta, scaffolding protein, membrane protein
• Biological source: Mus musculus (mouse)
• Cellular location: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P54116
• Total number of polymer chains: 2
• Total formula weight: 29738.23

Authors

Brand, J.,Schwefel, D.,Daumke, O. (deposition date: 2012-06-29, release date: 2012-08-15, Last modification date: 2023-09-13)

Primary citation

Brand, J.,Smith, E.S.,Schwefel, D.,Lapatsina, L.,Poole, K.,Omerbasic, D.,Kozlenkov, A.,Behlke, J.,Lewin, G.R.,Daumke, O.
A stomatin dimer modulates the activity of acid-sensing ion channels.
Embo J., 31:3635-3646, 2012

PubMed Abstract: Stomatin proteins oligomerize at membranes and have been implicated in ion channel regulation and membrane trafficking. To obtain mechanistic insights into their function, we determined three crystal structures of the conserved stomatin domain of mouse stomatin that assembles into a banana-shaped dimer. We show that dimerization is crucial for the repression of acid-sensing ion channel 3 (ASIC3) activity. A hydrophobic pocket at the inside of the concave surface is open in the presence of an internal peptide ligand and closes in the absence of this ligand, and we demonstrate a function of this pocket in the inhibition of ASIC3 activity. In one crystal form, stomatin assembles via two conserved surfaces into a cylindrical oligomer, and these oligomerization surfaces are also essential for the inhibition of ASIC3-mediated currents. The assembly mode of stomatin uncovered in this study might serve as a model to understand oligomerization processes of related membrane-remodelling proteins, such as flotillin and prohibitin.

PubMed: 22850675
DOI: 10.1038/emboj.2012.203

Experimental method

X-RAY DIFFRACTION (2.46 Å)