| http://purl.uniprot.org/citations/23587725 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23587725 | http://www.w3.org/2000/01/rdf-schema#comment | "The C-terminal soluble domain of stomatin operon partner protein (STOPP) of the hyperthermophilic archaeon Pyrococcus horikoshii has an oligonucleotide binding-fold (OB-fold). STOPP lacks the conserved surface residues necessary for binding to DNA/RNA. A tryptophan (W) residue is conserved instead at the molecular surface. Solvent-accessible W residues are often found at interfaces of protein-protein complexes, which suggested the possibility of self-assembling of STOPP. Protein-protein interactions among the C-terminal soluble domains of STOPP PH1510 (1510-C) were then analyzed by chemical linking and blue native polyacrylamide gel electrophoresis (BN-PAGE) methods. These results suggest that the soluble domains of STOPP could assemble into homo-oligomers. Since hexameric subcomplex I from archaeal proteasome consists of coiled-coil segments and OB-fold domains, molecular modeling of 1510-C was performed using hexameric subcomplex I as a template. Although 1510-C is a comparatively small polypeptide consisting of approximately 60 residues, numerous salt bridges and hydrophobic interactions were observed in the predicted hexamer of 1510-C, suggesting the stability of the homo-oligomeric structure. This oligomeric property of STOPP may be favorable for triplicate proteolysis of the trimer of prokaryotic stomatin."xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.biochi.2013.04.002"xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://purl.uniprot.org/core/author | "Forterre P."xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://purl.uniprot.org/core/author | "Yokoyama H."xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://purl.uniprot.org/core/author | "Matsui E."xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://purl.uniprot.org/core/author | "Matsui I."xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://purl.uniprot.org/core/author | "Hiramoto K."xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23587725 | http://purl.uniprot.org/core/name | "Biochimie"xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://purl.uniprot.org/core/pages | "1494-1501"xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://purl.uniprot.org/core/title | "Clustering of OB-fold domains of the partner protease complexed with trimeric stomatin from Thermococcales."xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://purl.uniprot.org/core/volume | "95"xsd:string |
| http://purl.uniprot.org/citations/23587725 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23587725 |
| http://purl.uniprot.org/citations/23587725 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23587725 |
| http://purl.uniprot.org/uniprot/#_O59179-mappedCitation-23587725 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23587725 |
| http://purl.uniprot.org/uniprot/O59179 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/23587725 |