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
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.
Clustering of OB-fold domains of the partner protease complexed with trimeric stomatin from Thermococcales.,Yokoyama H, Matsui E, Hiramoto K, Forterre P, Matsui I Biochimie. 2013 Jul;95(7):1494-501. doi: 10.1016/j.biochi.2013.04.002. Epub 2013 , Apr 12. PMID:23587725[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 E, Hiramoto K, Forterre P, Matsui I. Clustering of OB-fold domains of the partner protease complexed with trimeric stomatin from Thermococcales. Biochimie. 2013 Jul;95(7):1494-501. doi: 10.1016/j.biochi.2013.04.002. Epub 2013 , Apr 12. PMID:23587725 doi:http://dx.doi.org/10.1016/j.biochi.2013.04.002
