Crystallization (Comment) | Organism |
---|---|
purified recombinant C-terminal soluble domain 1510-C of STOPP PH1510, sitting drop vapor diffusion method, mixing of 0.0005 ml of 5.7 mg/ml protein in 50 mM Tris-HCl, pH 7.5, and 50 mM NaCl with 0.0005 ml of reservoir solution containing 20% v/v Jeffamine M-600 and 0.1 M HEPES-NaOH, pH 7.5, 20°C, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement, for modelling the structure with PDB ID 2EXD is used method | Pyrococcus horikoshii |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Pyrococcus horikoshii | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O59179 | - |
- |
Subunits | Comment | Organism |
---|---|---|
multimer | the structure of C-terminal soluble enzyme domain 1510-C, residues 371-441 of PH1510, has a compact five-stranded beta-barrel fold known as an oligosaccharide/oligonucleotide-binding fold (OB-fold). According to crystal packing, 1510-C can assemble into multimers based on a dimer as a basic unit. C-terminal soluble enzyme domain 1510-C also forms a large cylinder-like structure composed of 24 subunits or a large triangular prism-like structure composed of 12 subunits | Pyrococcus horikoshii |
Synonyms | Comment | Organism |
---|---|---|
stomatin operon partner protein | - |
Pyrococcus horikoshii |
Stomatin/STOPP | - |
Pyrococcus horikoshii |
STOPP PH1510 | - |
Pyrococcus horikoshii |
General Information | Comment | Organism |
---|---|---|
additional information | C-terminal soluble enzyme domain 1510-C, residues 371-441 of PH1510, functions as a scaffold protein to form the multimeric assembly of STOPP and stomatin | Pyrococcus horikoshii |
physiological function | the enzyme may be involved in the quality control of membrane proteins, e.g. stomatin, prohibitin, flotillin, and HflK/C domain proteins found in the lipid raft microdomains of various cellular membranes | Pyrococcus horikoshii |