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Literature summary for 3.4.21.B56 extracted from

  • Yokoyama, H.; Matsui, I.
    Crystal structure of the stomatin operon partner protein from Pyrococcus horikoshii indicates the formation of a multimeric assembly (2014), FEBS open bio, 4, 804-812.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Pyrococcus horikoshii 16020
-

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O59179
-
-

Subunits

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

Synonyms Comment Organism
stomatin operon partner protein
-
Pyrococcus horikoshii
Stomatin/STOPP
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Pyrococcus horikoshii
STOPP PH1510
-
Pyrococcus horikoshii

General Information

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