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| | <StructureSection load='3bpp' size='340' side='right'caption='[[3bpp]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3bpp' size='340' side='right'caption='[[3bpp]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3bpp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BPP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3bpp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BPP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2deo|2deo]]</div></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]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PH1510 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53953 'Pyrococcus shinkaii'])</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=3bpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bpp OCA], [https://pdbe.org/3bpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bpp RCSB], [https://www.ebi.ac.uk/pdbsum/3bpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bpp 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=3bpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bpp OCA], [https://pdbe.org/3bpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bpp RCSB], [https://www.ebi.ac.uk/pdbsum/3bpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bpp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pyrococcus shinkaii]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fujii, S]] | + | [[Category: Pyrococcus horikoshii]] |
| - | [[Category: Hamamatsu, S]] | + | [[Category: Fujii S]] |
| - | [[Category: Matsui, I]] | + | [[Category: Hamamatsu S]] |
| - | [[Category: Yokoyama, H]] | + | [[Category: Matsui I]] |
| - | [[Category: Archaea]]
| + | [[Category: Yokoyama H]] |
| - | [[Category: Catalytic dyad]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Membrane protease]]
| + | |
| - | [[Category: Pyrococcus]]
| + | |
| - | [[Category: Specific for a stomatin homolog]]
| + | |
| - | [[Category: Thermostable]]
| + | |
| 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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Membrane-bound proteases are involved in various regulatory functions. A previous report indicates that the N-terminal region of PH1510 (1510-N) from the hyperthermophilic archaeon Pyrococcus horikoshii is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138), and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511. According to the crystal structure of the wild-type 1510-N in dimeric form, the active site around Ser97 is in a hydrophobic environment suitable for the hydrophobic substrates. This article reports the crystal structure of the K138A mutant of 1510-N at 2.3 A resolution. The determined structure contains one molecule per asymmetric unit, but 1510-N is active in dimeric form. Two possible sets of dimer were found from the symmetry-related molecules. One dimer is almost the same as the wild-type 1510-N. Another dimer is probably in an inactive form. The L2 loop, which is disordered in the wild-type structure, is significantly kinked at around A-138 in the K138A mutant. Thus Lys138 probably has an important role on the conformation of L2.
Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin.,Yokoyama H, Hamamatsu S, Fujii S, Matsui I J Synchrotron Radiat. 2008 May;15(Pt 3):254-7. Epub 2008 Apr 18. PMID:18421152[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, Hamamatsu S, Fujii S, Matsui I. Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin. J Synchrotron Radiat. 2008 May;15(Pt 3):254-7. Epub 2008 Apr 18. PMID:18421152 doi:10.1107/S0909049507068471
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