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| | ==The prostaphopain B structure== | | ==The prostaphopain B structure== |
| - | <StructureSection load='1x9y' size='340' side='right' caption='[[1x9y]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='1x9y' size='340' side='right'caption='[[1x9y]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1x9y]] is a 4 chain structure with sequence from [http://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=1X9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X9Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1x9y]] is a 4 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=1X9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X9Y FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cv8|1cv8]], [[1pxv|1pxv]]</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]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sspB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=1x9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9y OCA], [https://pdbe.org/1x9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x9y RCSB], [https://www.ebi.ac.uk/pdbsum/1x9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x9y ProSAT]</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=1x9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9y OCA], [http://pdbe.org/1x9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x9y RCSB], [http://www.ebi.ac.uk/pdbsum/1x9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x9y ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SSPB_STAAU SSPB_STAAU]] Cysteine protease able to degrade elastin, fibrogen, fibronectin and kininogen. Exhibits a strong preference for substrates where arginine is preceded by a hydrophobic amino acid. Promotes detachment of primary human keratinocytes. Along with other extracellular proteases is involved in colonization and infection of human tissues (By similarity). | + | [https://www.uniprot.org/uniprot/SSPB_STAAU SSPB_STAAU] Cysteine protease able to degrade elastin, fibrogen, fibronectin and kininogen. Exhibits a strong preference for substrates where arginine is preceded by a hydrophobic amino acid. Promotes detachment of primary human keratinocytes. Along with other extracellular proteases is involved in colonization and infection of human tissues (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1x9y" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1x9y" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Proteinase 3D structures|Proteinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bochtler, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Filipek, R]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Potempa, J]] | + | [[Category: Bochtler M]] |
| - | [[Category: Sabat, A]] | + | [[Category: Filipek R]] |
| - | [[Category: Szczepanowski, R]]
| + | [[Category: Potempa J]] |
| - | [[Category: Barrel-sandwich-hybrid]] | + | [[Category: Sabat A]] |
| - | [[Category: Half-barrel]] | + | [[Category: Szczepanowski R]] |
| - | [[Category: Hydrolase]] | + | |
| Structural highlights
Function
SSPB_STAAU Cysteine protease able to degrade elastin, fibrogen, fibronectin and kininogen. Exhibits a strong preference for substrates where arginine is preceded by a hydrophobic amino acid. Promotes detachment of primary human keratinocytes. Along with other extracellular proteases is involved in colonization and infection of human tissues (By similarity).
Publication Abstract from PubMed
Prostaphopain B is the precursor of staphopain B, a papain-type secreted cysteine protease from the pathogen Staphylococcus aureus. Here, we describe the 2.5 A crystal structure of the proenzyme. Its 21 kDa proregion is organized around a central half-barrel or barrel-sandwich hybrid and occludes primed, but not nonprimed, sites in the active site cleft of the protease. The structure of the mature part of the protease is similar to previously reported staphopain structures, and no distortion of the catalytic residues is apparent at 2.5 A resolution. A comparison of prostaphopain B with the staphopain B-staphostatin B complex shows that the proregion and the inhibitor interact with largely nonoverlapping parts of the protease surface. In a modeled complex of prostaphopain B with staphostatin B, clashes occur both inside and outside the active site cleft, but involve mostly poorly ordered regions of the protein that may be mobile.
Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition.,Filipek R, Szczepanowski R, Sabat A, Potempa J, Bochtler M Biochemistry. 2004 Nov 9;43(44):14306-15. PMID:15518582[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Filipek R, Szczepanowski R, Sabat A, Potempa J, Bochtler M. Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition. Biochemistry. 2004 Nov 9;43(44):14306-15. PMID:15518582 doi:10.1021/bi048661m
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