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| | <StructureSection load='3afg' size='340' side='right'caption='[[3afg]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3afg' size='340' side='right'caption='[[3afg]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3afg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermococcus_kodakaraensis"_atomi_et_al._2004 "thermococcus kodakaraensis" atomi et al. 2004]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AFG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3afg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AFG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1scj|1scj]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TK1689 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=311400 "Thermococcus kodakaraensis" Atomi et al. 2004])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </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=3afg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3afg OCA], [https://pdbe.org/3afg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3afg RCSB], [https://www.ebi.ac.uk/pdbsum/3afg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3afg 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=3afg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3afg OCA], [https://pdbe.org/3afg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3afg RCSB], [https://www.ebi.ac.uk/pdbsum/3afg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3afg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Q5JIZ5_THEKO Q5JIZ5_THEKO]] Serine protease with a broad substrate specificity.<ref>PMID:20100702</ref>
| + | [https://www.uniprot.org/uniprot/TKSP_THEKO TKSP_THEKO] Serine protease with a broad substrate specificity.<ref>PMID:20100702</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: Thermococcus kodakaraensis atomi et al. 2004]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Subtilisin]] | + | [[Category: Thermococcus kodakarensis]] |
| - | [[Category: Angkawidjaja, C]] | + | [[Category: Angkawidjaja C]] |
| - | [[Category: Foophow, T]] | + | [[Category: Foophow T]] |
| - | [[Category: Kanaya, S]] | + | [[Category: Kanaya S]] |
| - | [[Category: Koga, Y]] | + | [[Category: Koga Y]] |
| - | [[Category: Takano, K]] | + | [[Category: Takano K]] |
| - | [[Category: Tanaka, S]] | + | [[Category: Tanaka S]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Propeptide]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| - | [[Category: Thermococcus kodakaraensis]]
| + | |
| Structural highlights
Function
TKSP_THEKO Serine protease with a broad substrate specificity.[1]
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
Tk-SP is a hyperthermostable subtilisin-like serine protease from Thermococcus kodakaraensis and is autoprocessed from its precursor (Pro-Tk-SP) with N- and C-propeptides. The crystal structure of the active-site mutant of Pro-Tk-SP lacking C-propeptide, ProN-Tk-S359A, was determined at 2.0 A resolution. ProN-Tk-S359A consists of the N-propeptide, subtilisin, and beta-jelly roll domains. Two Ca(2+) ions bind to the beta-jelly roll domain. The overall structure of ProN-Tk-S359A without the beta-jelly roll domain is similar to that of the bacterial propeptide:subtilisin complex, except that it does not contain Ca(2+) ions. To analyze the role of the beta-jelly roll domain of Tk-SP, we constructed a series of the active-site mutants of Tk-SP with (Tk-S359A/C) and without (Tk-S359A/CDeltaJ) beta-jelly roll domain. Both Tk-S359C and Tk-S359CDeltaJ exhibited protease activities in gel assay, indicating that the beta-jelly roll domain is not required for folding or activity. However, the T(m) value of Tk-S359ADeltaJ determined by far-UV CD spectroscopy in the presence of 10-mM CaCl(2) was lower than that of Tk-S359A by 29.4 degrees C. The T(m) value of Tk-S359A was decreased by 29.5 degrees C by the treatment with 10 mM ethylenediaminetetraacetic acid, indicating that the beta-jelly roll domain contributes to the stabilization of Tk-S359A only in a Ca(2+)-bound form. Tk-SP highly resembles subtilisin-like serine proteases from Pyrococcus furiosus, Thermococcus gammatolerans, and Thermococcus onnurineus in size and amino acid sequence. We propose that attachment of a beta-jelly roll domain to the C-terminus is one of the strategies of the proteins from hyperthermophiles to adapt to high-temperature environment.
Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis: requirement of a C-terminal beta-jelly roll domain for hyperstability.,Foophow T, Tanaka S, Angkawidjaja C, Koga Y, Takano K, Kanaya S J Mol Biol. 2010 Jul 23;400(4):865-77. Epub 2010 Jun 1. PMID:20595040[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Foophow T, Tanaka S, Koga Y, Takano K, Kanaya S. Subtilisin-like serine protease from hyperthermophilic archaeon Thermococcus kodakaraensis with N- and C-terminal propeptides. Protein Eng Des Sel. 2010 May;23(5):347-55. doi: 10.1093/protein/gzp092. Epub, 2010 Jan 25. PMID:20100702 doi:http://dx.doi.org/10.1093/protein/gzp092
- ↑ Foophow T, Tanaka S, Angkawidjaja C, Koga Y, Takano K, Kanaya S. Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis: requirement of a C-terminal beta-jelly roll domain for hyperstability. J Mol Biol. 2010 Jul 23;400(4):865-77. Epub 2010 Jun 1. PMID:20595040 doi:10.1016/j.jmb.2010.05.064
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