3WWV

C-terminal domain of stomatin operon partner protein 1510-C from Pyrococcus horikoshii

Summary for 3WWV

• Entry DOI: 10.2210/pdb3wwv/pdb
• Related: 2DEO 2EXD 3BK6 3BPP 3VIV 3WG5
• Descriptor: Stomatin operon partner protein, SODIUM ION (3 entities in total)
• Functional Keywords: beta barrel, ob fold, unknown function, membrane protein stomatin
• Biological source: Pyrococcus horikoshii OT3
• Cellular location: Membrane ; Multi-pass membrane protein : O59179
• Total number of polymer chains: 1
• Total formula weight: 9208.72

Authors

Yokoyama, H.,Matsui, I. (deposition date: 2014-06-30, release date: 2014-10-01, Last modification date: 2023-11-08)

Primary citation

Yokoyama, H.,Matsui, I.
Crystal structure of the stomatin operon partner protein from Pyrococcus horikoshii indicates the formation of a multimeric assembly
FEBS Open Bio, 4:804-812, 2014

PubMed Abstract: Stomatin, prohibitin, flotillin, and HflK/C (SPFH) domain proteins are found in the lipid raft microdomains of various cellular membranes. Stomatin/STOPP (stomatin operon partner protein) gene pairs are present in both archaeal and bacterial species, and their protein products may be involved in the quality control of membrane proteins. In the present study, the crystal structure of the C-terminal soluble domain of STOPP PH1510 (1510-C) from the hyperthermophilic archaeon Pyrococcus horikoshii was determined at 2.4 Å resolution. The structure of 1510-C had a compact five-stranded β-barrel fold known as an oligosaccharide/oligonucleotide-binding fold (OB-fold). According to crystal packing, 1510-C could assemble into multimers based on a dimer as a basic unit. 1510-C also formed a large cylinder-like structure composed of 24 subunits or a large triangular prism-like structure composed of 12 subunits. These results indicate that 1510-C functions as a scaffold protein to form the multimeric assembly of STOPP and stomatin.

PubMed: 25349784
DOI: 10.1016/j.fob.2014.09.002

Experimental method

X-RAY DIFFRACTION (2.4 Å)