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C-terminal domain of stomatin operon partner protein 1510-C from Pyrococcus horikoshii
Structural highlights
FunctionSTOPP_PYRHO Protease that cleaves its substrates preferentially near hydrophobic or aromatic amino acid residues. Can degrade casein and the stomatin homolog PH1511 (in vitro).[1] [2] [3] Publication Abstract from PubMedStomatin, 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 A resolution. The structure of 1510-C had a compact five-stranded beta-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. Crystal structure of the stomatin operon partner protein from Pyrococcus horikoshii indicates the formation of a multimeric assembly.,Yokoyama H, Matsui I FEBS Open Bio. 2014 Sep 16;4:804-12. doi: 10.1016/j.fob.2014.09.002. eCollection , 2014. PMID:25349784[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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