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2o8l

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Current revision (10:33, 30 August 2023) (edit) (undo)
 
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<StructureSection load='2o8l' size='340' side='right'caption='[[2o8l]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2o8l' size='340' side='right'caption='[[2o8l]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2o8l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O8L FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2o8l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O8L FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qy6|1qy6]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamyl_endopeptidase Glutamyl endopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.19 3.4.21.19] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o8l OCA], [https://pdbe.org/2o8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o8l RCSB], [https://www.ebi.ac.uk/pdbsum/2o8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o8l 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=2o8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o8l OCA], [https://pdbe.org/2o8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o8l RCSB], [https://www.ebi.ac.uk/pdbsum/2o8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o8l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/SSPA_STAAM SSPA_STAAM]] Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).
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[https://www.uniprot.org/uniprot/SSPA_STAAM SSPA_STAAM] Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases (By similarity).
== 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>
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[[Category: Glutamyl endopeptidase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Delbaere, L T.J]]
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[[Category: Staphylococcus aureus]]
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[[Category: Leduc, Y]]
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[[Category: Delbaere LTJ]]
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[[Category: Prasad, L]]
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[[Category: Leduc Y]]
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[[Category: Enzyme]]
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[[Category: Prasad L]]
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[[Category: Hydrolase]]
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[[Category: Serine protease]]
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Current revision

Structure of V8 protease from staphylococcus aureus

PDB ID 2o8l

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