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| | <StructureSection load='1y4d' size='340' side='right'caption='[[1y4d]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1y4d' size='340' side='right'caption='[[1y4d]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1y4d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943] and [https://en.wikipedia.org/wiki/Barley Barley]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y4D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1y4d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] and [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y4D 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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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;'>[[1y1k|1y1k]], [[1y33|1y33]], [[1y34|1y34]], [[1y3b|1y3b]], [[1y3c|1y3c]], [[1y3d|1y3d]], [[1y3f|1y3f]], [[1y48|1y48]], [[1y4a|1y4a]]</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">apr ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 "Bacillus amyloliquifaciens" (sic) Fukumoto 1943])</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=1y4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4d OCA], [https://pdbe.org/1y4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y4d RCSB], [https://www.ebi.ac.uk/pdbsum/1y4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y4d 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=1y4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y4d OCA], [https://pdbe.org/1y4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y4d RCSB], [https://www.ebi.ac.uk/pdbsum/1y4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y4d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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: Barley]] | + | [[Category: Bacillus amyloliquefaciens]] |
| | + | [[Category: Hordeum vulgare]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Subtilisin]]
| + | [[Category: Koshland Jr DE]] |
| - | [[Category: Koshland, D E]] | + | [[Category: Kwan G]] |
| - | [[Category: Kwan, G]] | + | [[Category: Lu CJ]] |
| - | [[Category: Lu, C J]] | + | [[Category: Radisky ES]] |
| - | [[Category: Radisky, E S]] | + | |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| 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
A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues involved in intramolecular interactions that shape and constrain the binding loop, were studied to determine their relative importance for inhibition of the serine protease subtilisin BPN', and for resistance of the inhibitor to proteolysis. These functional properties were investigated in tandem with the crystal structures of the mutant inhibitor-enzyme complexes. A dense hydrogen bonding network that supports the binding loop in the vicinity of the scissile bond was found to be important both for enzyme affinity and for stability to proteolysis. Structural analysis, in combination with biochemical measurements, allows differentiation of the structural components most important for resistance to proteolysis and/or binding. The most critical participating residues in the network were found to be Thr-58, Glu-60, Arg-65, and Gly-83. Glu-60 is more important for resistance to proteolysis than for binding, while Arg-65 and two other Arg residues play a greater role in binding than in resistance to proteolysis. Structural comparisons reveal a wide variety of subtle conformational changes in response to mutation, with built-in robustness in the hydrogen bond network, such that loss of one contact is compensated by other new contacts.
Role of the intramolecular hydrogen bond network in the inhibitory power of chymotrypsin inhibitor 2.,Radisky ES, Lu CJ, Kwan G, Koshland DE Jr Biochemistry. 2005 May 10;44(18):6823-30. PMID:15865427[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
- ↑ Radisky ES, Lu CJ, Kwan G, Koshland DE Jr. Role of the intramolecular hydrogen bond network in the inhibitory power of chymotrypsin inhibitor 2. Biochemistry. 2005 May 10;44(18):6823-30. PMID:15865427 doi:http://dx.doi.org/10.1021/bi047301w
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