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| | <StructureSection load='1gns' size='340' side='right'caption='[[1gns]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1gns' size='340' side='right'caption='[[1gns]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gns]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GNS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1GNS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gns]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GNS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</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]] 1.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a2q|1a2q]], [[1ak9|1ak9]], [[1aqn|1aqn]], [[1au9|1au9]], [[1gnv|1gnv]], [[1s01|1s01]], [[1s02|1s02]], [[1sbh|1sbh]], [[1sbi|1sbi]], [[1sbn|1sbn]], [[1sbt|1sbt]], [[1sib|1sib]], [[1spb|1spb]], [[1st2|1st2]], [[1sua|1sua]], [[1sub|1sub]], [[1suc|1suc]], [[1sud|1sud]], [[1sue|1sue]], [[1sup|1sup]], [[1ubn|1ubn]], [[1yja|1yja]], [[1yjb|1yjb]], [[1yjc|1yjc]], [[2sbt|2sbt]], [[2sic|2sic]], [[2sni|2sni]], [[2st1|2st1]], [[3sic|3sic]], [[5sic|5sic]]</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=1gns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gns OCA], [https://pdbe.org/1gns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gns RCSB], [https://www.ebi.ac.uk/pdbsum/1gns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gns 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://proteopedia.org/fgij/fg.htm?mol=1gns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gns OCA], [http://pdbe.org/1gns PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gns RCSB], [http://www.ebi.ac.uk/pdbsum/1gns PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gns ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SUBT_BACAM SUBT_BACAM]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.<ref>PMID:12524032</ref> | + | [https://www.uniprot.org/uniprot/SUBT_BACAM SUBT_BACAM] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.<ref>PMID:12524032</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: Bacillus amyloliquefaciens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Subtilisin]]
| + | [[Category: Alexander P]] |
| - | [[Category: Alexander, P]] | + | [[Category: Almog O]] |
| - | [[Category: Almog, O]] | + | [[Category: Gallagher DT]] |
| - | [[Category: Gallagher, D T]] | + | [[Category: Ladner JE]] |
| - | [[Category: Ladner, J E]] | + | [[Category: Strausberg S]] |
| - | [[Category: Strausberg, S]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Serine proteinase]]
| + | |
| Structural highlights
Function
SUBT_BACAM Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.[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
The crystal structures of two thermally stabilized subtilisin BPN' variants, S63 and S88, are reported here at 1.8 and 1.9 A resolution, respectively. The micromolar affinity calcium binding site (site A) has been deleted (Delta75-83) in these variants, enabling the activity and thermostability measurements in chelating conditions. Each of the variants includes mutations known previously to increase the thermostability of calcium-independent subtilisin in addition to new stabilizing mutations. S63 has eight amino acid replacements: D41A, M50F, A73L, Q206W, Y217K, N218S, S221C, and Q271E. S63 has 75-fold greater stability than wild type subtilisin in chelating conditions (10 mm EDTA). The other variant, S88, has ten site-specific changes: Q2K, S3C, P5S, K43N, M50F, A73L, Q206C, Y217K, N218S, and Q271E. The two new cysteines form a disulfide bond, and S88 has 1000 times greater stability than wild type subtilisin in chelating conditions. Comparisons of the two new crystal structures (S63 in space group P2(1) with A cell constants 41.2, 78.1, 36.7, and beta = 114.6 degrees and S88 in space group P2(1)2(1)2(1) with cell constants 54.2, 60.4, and 82.7) with previous structures of subtilisin BPN' reveal that the principal changes are in the N-terminal region. The structural bases of the stabilization effects of the new mutations Q2K, S3C, P5S, D41A, Q206C, and Q206W are generally apparent. The effects are attributed to the new disulfide cross-link and to improved hydrophobic packing, new hydrogen bonds, and other rearrangements in the N-terminal region.
Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'.,Almog O, Gallagher DT, Ladner JE, Strausberg S, Alexander P, Bryan P, Gilliland GL J Biol Chem. 2002 Jul 26;277(30):27553-8. Epub 2002 May 13. PMID:12011071[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Peng Y, Huang Q, Zhang RH, Zhang YZ. Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food. Comp Biochem Physiol B Biochem Mol Biol. 2003 Jan;134(1):45-52. PMID:12524032
- ↑ Almog O, Gallagher DT, Ladner JE, Strausberg S, Alexander P, Bryan P, Gilliland GL. Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'. J Biol Chem. 2002 Jul 26;277(30):27553-8. Epub 2002 May 13. PMID:12011071 doi:10.1074/jbc.M111777200
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