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| | ==Crystal structure of an intracellular proteinase inhibitor (ipi, bsu11130) from bacillus subtilis at 2.61 A resolution== | | ==Crystal structure of an intracellular proteinase inhibitor (ipi, bsu11130) from bacillus subtilis at 2.61 A resolution== |
| - | <StructureSection load='3isy' size='340' side='right' caption='[[3isy]], [[Resolution|resolution]] 2.61Å' scene=''> | + | <StructureSection load='3isy' size='340' side='right'caption='[[3isy]], [[Resolution|resolution]] 2.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3isy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ISY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ISY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3isy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ISY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ISY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 2.61Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU11130, ipi, NP_388994.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=3isy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3isy OCA], [https://pdbe.org/3isy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3isy RCSB], [https://www.ebi.ac.uk/pdbsum/3isy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3isy ProSAT], [https://www.topsan.org/Proteins/JCSG/3isy TOPSAN]</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=3isy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3isy OCA], [http://pdbe.org/3isy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3isy RCSB], [http://www.ebi.ac.uk/pdbsum/3isy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3isy ProSAT], [http://www.topsan.org/Proteins/JCSG/3isy TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IPI_BACSU IPI_BACSU]] Directly regulates the major intracellular proteinase (ISP-1) activity in vivo. Inhibits ISP-1 in the early stages of sporulation. It may be then inactivated by a membrane-bound proteinase. | + | [https://www.uniprot.org/uniprot/IPI_BACSU IPI_BACSU] Directly regulates the major intracellular proteinase (ISP-1) activity in vivo. Inhibits ISP-1 in the early stages of sporulation. It may be then inactivated by a membrane-bound proteinase. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/is/3isy_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/is/3isy_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Structural genomic]] | + | [[Category: Large Structures]] |
| - | [[Category: Beta sandwich]]
| + | |
| - | [[Category: Greek key]]
| + | |
| - | [[Category: Intracellular proteinase inhibitor bsupi]]
| + | |
| - | [[Category: Jcsg]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| Structural highlights
Function
IPI_BACSU Directly regulates the major intracellular proteinase (ISP-1) activity in vivo. Inhibits ISP-1 in the early stages of sporulation. It may be then inactivated by a membrane-bound proteinase.
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
We report the crystal structure solution of the Intracellular Protease Inhibitor (IPI) protein from Bacillus subtilis, which has been reported to be an inhibitor of the intracellular subtilisin Isp1 from the same organism. The structure of IPI is a variant of the all-beta, immunoglobulin (Ig) fold. It is possible that IPI is important for protein-protein interactions, of which inhibition of Isp1 is one. The intracellular nature of ISP is questioned, because an alternative ATG codon in the ipi gene would produce a protein with an N-terminal extension containing a signal peptide. It is possible that alternative initiation exists, producing either an intracellular inhibitor or a secreted form that may be associated with the cell surface. Homologues of the IPI protein from other species are multi-domain proteins, containing signal peptides and domains also associated with the bacterial cell-surface. The cysteine peptidase inhibitors chagasin and amoebiasin also have Ig-like folds, but their topology differs significantly from that of IPI, and they share no recent common ancestor. A model of IPI docked to Isp1 shows similarities to other subtilisin:inhibitor complexes, particularly where the inhibitor interacts with the peptidase active site.
The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold.,Rigden DJ, Xu Q, Chang Y, Eberhardt RY, Finn RD, Rawlings ND F1000Res. 2013 Jul 10;2:154. doi: 10.12688/f1000research.2-154.v2. eCollection, 2013. PMID:24555072[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rigden DJ, Xu Q, Chang Y, Eberhardt RY, Finn RD, Rawlings ND. The first structure in a family of peptidase inhibitors reveals an unusual Ig-like fold. F1000Res. 2013 Jul 10;2:154. doi: 10.12688/f1000research.2-154.v2. eCollection, 2013. PMID:24555072 doi:http://dx.doi.org/10.12688/f1000research.2-154.v2
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