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| | <StructureSection load='3bx1' size='340' side='right'caption='[[3bx1]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='3bx1' size='340' side='right'caption='[[3bx1]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3bx1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus] and [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BX1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3BX1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3bx1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] and [https://en.wikipedia.org/wiki/Lederbergia_lenta Lederbergia lenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BX1 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=CL:CHLORIDE+ION'>CL</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]] 1.85Å</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='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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=3bx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bx1 OCA], [http://pdbe.org/3bx1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bx1 RCSB], [http://www.ebi.ac.uk/pdbsum/3bx1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bx1 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=3bx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bx1 OCA], [https://pdbe.org/3bx1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bx1 RCSB], [https://www.ebi.ac.uk/pdbsum/3bx1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bx1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SUBS_BACLE SUBS_BACLE]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. [[http://www.uniprot.org/uniprot/IAAS_HORVU IAAS_HORVU]] This protein inhibits independently subtilisin and alpha-amylase. | + | [https://www.uniprot.org/uniprot/SUBS_LEDLE SUBS_LEDLE] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. |
| | == 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 lentus]] | |
| | [[Category: Hordeum vulgare]] | | [[Category: Hordeum vulgare]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Subtilisin]] | + | [[Category: Lederbergia lenta]] |
| - | [[Category: Micheelsen, P O]] | + | [[Category: Micheelsen PO]] |
| - | [[Category: Skjot, M]] | + | [[Category: Skjot M]] |
| - | [[Category: Vevodova, J]] | + | [[Category: Vevodova J]] |
| - | [[Category: Wilson, K]] | + | [[Category: Wilson K]] |
| - | [[Category: Alpha-amylase inhibitor]]
| + | |
| - | [[Category: Barley alpha-amylase/subtilisin inhibitor]]
| + | |
| - | [[Category: Calcium]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Protease inhibitor]]
| + | |
| - | [[Category: Savinase]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| - | [[Category: Serine protease inhibitor]]
| + | |
| - | [[Category: Sporulation]]
| + | |
| Structural highlights
Function
SUBS_LEDLE Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
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
Subtilisins represent a large class of microbial serine proteases. To date, there are three-dimensional structures of proteinaceous inhibitors from three families in complex with subtilisins in the Protein Data Bank. All interact with subtilisin via an exposed loop covering six interacting residues. Here we present the crystal structure of the complex between the Bacillus lentus subtilisin Savinase and the barley alpha-amylase/subtilisin inhibitor (BASI). This is the first reported structure of a cereal Kunitz-P family inhibitor in complex with a subtilisin. Structural analysis revealed that BASI inhibits Savinase in a novel way, as the interacting loop is shorter than loops previously reported. Mutational analysis showed that Thr88 is crucial for the inhibition, as it stabilises the interacting loop through intramolecular interactions with the BASI backbone.
Structural and mutational analyses of the interaction between the barley alpha-amylase/subtilisin inhibitor and the subtilisin savinase reveal a novel mode of inhibition.,Micheelsen PO, Vevodova J, De Maria L, Ostergaard PR, Friis EP, Wilson K, Skjot M J Mol Biol. 2008 Jul 18;380(4):681-90. Epub 2008 May 22. PMID:18556023[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Micheelsen PO, Vevodova J, De Maria L, Ostergaard PR, Friis EP, Wilson K, Skjot M. Structural and mutational analyses of the interaction between the barley alpha-amylase/subtilisin inhibitor and the subtilisin savinase reveal a novel mode of inhibition. J Mol Biol. 2008 Jul 18;380(4):681-90. Epub 2008 May 22. PMID:18556023 doi:10.1016/j.jmb.2008.05.034
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