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| | ==C-terminal domain of stomatin operon partner protein 1510-C from Pyrococcus horikoshii== | | ==C-terminal domain of stomatin operon partner protein 1510-C from Pyrococcus horikoshii== |
| - | <StructureSection load='3wwv' size='340' side='right' caption='[[3wwv]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='3wwv' size='340' side='right'caption='[[3wwv]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wwv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WWV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wwv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WWV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2exd|2exd]], [[3wg5|3wg5]], [[3viv|3viv]], [[3bpp|3bpp]], [[2deo|2deo]], [[3bk6|3bk6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wwv OCA], [http://pdbe.org/3wwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wwv RCSB], [http://www.ebi.ac.uk/pdbsum/3wwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wwv ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wwv OCA], [https://pdbe.org/3wwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wwv RCSB], [https://www.ebi.ac.uk/pdbsum/3wwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wwv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/STOPP_PYRHO STOPP_PYRHO]] Protease that cleaves its substrates preferentially near hydrophobic or aromatic amino acid residues. Can degrade casein and the stomatin homolog PH1511 (in vitro).<ref>PMID:15611110</ref> <ref>PMID:16574150</ref> <ref>PMID:24121343</ref> | + | [https://www.uniprot.org/uniprot/STOPP_PYRHO STOPP_PYRHO] Protease that cleaves its substrates preferentially near hydrophobic or aromatic amino acid residues. Can degrade casein and the stomatin homolog PH1511 (in vitro).<ref>PMID:15611110</ref> <ref>PMID:16574150</ref> <ref>PMID:24121343</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Matsui, I]] | + | [[Category: Large Structures]] |
| - | [[Category: Yokoyama, H]] | + | [[Category: Pyrococcus horikoshii OT3]] |
| - | [[Category: Beta barrel]] | + | [[Category: Matsui I]] |
| - | [[Category: Membrane protein stomatin]] | + | [[Category: Yokoyama H]] |
| - | [[Category: Ob fold]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
STOPP_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 PubMed
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 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
- ↑ Yokoyama H, Matsui I. A novel thermostable membrane protease forming an operon with a stomatin homolog from the hyperthermophilic archaebacterium Pyrococcus horikoshii. J Biol Chem. 2005 Feb 25;280(8):6588-94. Epub 2004 Dec 16. PMID:15611110 doi:10.1074/jbc.M411748200
- ↑ Yokoyama H, Matsui E, Akiba T, Harata K, Matsui I. Molecular structure of a novel membrane protease specific for a stomatin homolog from the hyperthermophilic archaeon Pyrococcus horikoshii. J Mol Biol. 2006 May 12;358(4):1152-64. Epub 2006 Mar 9. PMID:16574150 doi:10.1016/j.jmb.2006.02.052
- ↑ Yokoyama H, Kobayashi D, Takizawa N, Fujii S, Matsui I. Structural and biochemical analysis of a thermostable membrane-bound stomatin-specific protease. J Synchrotron Radiat. 2013 Nov;20(Pt 6):933-7. doi: 10.1107/S0909049513021328., Epub 2013 Sep 25. PMID:24121343 doi:http://dx.doi.org/10.1107/S0909049513021328
- ↑ 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. 2014 Sep 16;4:804-12. doi: 10.1016/j.fob.2014.09.002. eCollection , 2014. PMID:25349784 doi:http://dx.doi.org/10.1016/j.fob.2014.09.002
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