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| | ==Crystal structure of S324A-subtilisin== | | ==Crystal structure of S324A-subtilisin== |
| - | <StructureSection load='2zrq' size='340' side='right' caption='[[2zrq]], [[Resolution|resolution]] 2.16Å' scene=''> | + | <StructureSection load='2zrq' size='340' side='right'caption='[[2zrq]], [[Resolution|resolution]] 2.16Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zrq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZRQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZRQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zrq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZRQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.16Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2z2x|2z2x]]</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">TK1675 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</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=2zrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zrq OCA], [https://pdbe.org/2zrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zrq RCSB], [https://www.ebi.ac.uk/pdbsum/2zrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zrq ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zrq OCA], [http://pdbe.org/2zrq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zrq RCSB], [http://www.ebi.ac.uk/pdbsum/2zrq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zrq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TKSU_THEKO TKSU_THEKO]] Has a broad substrate specificity with a slight preference to large hydrophobic amino acid residues at the P1 position. | + | [https://www.uniprot.org/uniprot/TKSU_THEKO TKSU_THEKO] Has a broad substrate specificity with a slight preference to large hydrophobic amino acid residues at the P1 position. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Subtilisin|Subtilisin]] | + | *[[Subtilisin 3D structures|Subtilisin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Subtilisin]] | + | [[Category: Large Structures]] |
| - | [[Category: Kanaya, S]] | + | [[Category: Thermococcus kodakarensis KOD1]] |
| - | [[Category: Koga, Y]] | + | [[Category: Kanaya S]] |
| - | [[Category: Matsumura, H]] | + | [[Category: Koga Y]] |
| - | [[Category: Takano, K]] | + | [[Category: Matsumura H]] |
| - | [[Category: Takeuchi, Y]] | + | [[Category: Takano K]] |
| - | [[Category: Tanaka, S]] | + | [[Category: Takeuchi Y]] |
| - | [[Category: Calcium]]
| + | [[Category: Tanaka S]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Serine protease]]
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| - | [[Category: Thermococcus kodakaraensis]]
| + | |
| - | [[Category: Zymogen]]
| + | |
| Structural highlights
Function
TKSU_THEKO Has a broad substrate specificity with a slight preference to large hydrophobic amino acid residues at the P1 position.
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-subtilisin (a subtilisin homologue from Thermococcus kodakaraensis) is matured from Pro-Tk-subtilisin upon autoprocessing and degradation of Tk-propeptide. To analyze the folding mechanism of Tk-subtilisin, the crystal structure of the active site mutant of Tk-subtilisin (S324A-subtilisin*), which was refolded in the presence of Ca2+ and absence of Tk-propeptide, was determined at 2.16A resolution. This structure is essentially the same as that of Tk-subtilisin matured from Pro-Tk-subtilisin. S324A-subtilisin* was refolded with a rate constant of 0.17 and 1.8min(-1) at 30 degrees C in the absence and presence of Tk-propeptide, respectively, indicating that Tk-subtilisin does not require Tk-propeptide for folding but requires it for acceleration of folding.
Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding.,Tanaka S, Takeuchi Y, Matsumura H, Koga Y, Takano K, Kanaya S FEBS Lett. 2008 Nov 26;582(28):3875-8. Epub 2008 Oct 23. PMID:18951896[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tanaka S, Takeuchi Y, Matsumura H, Koga Y, Takano K, Kanaya S. Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding. FEBS Lett. 2008 Nov 26;582(28):3875-8. Epub 2008 Oct 23. PMID:18951896 doi:10.1016/j.febslet.2008.10.025
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