1x9y: Difference between revisions
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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=''> | ||
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</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cv8|1cv8]], [[1pxv|1pxv]]</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='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'>[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]</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 == | ||
Revision as of 10:19, 18 April 2018
The prostaphopain B structureThe prostaphopain B structure
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 PubMedProstaphopain 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. References
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