1x9y: Difference between revisions

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-[[Image:1x9y.gif|left|200px]]
- {{Structure
+==The prostaphopain B structure==
-|PDB= 1x9y |SIZE=350|CAPTION= <scene name='initialview01'>1x9y</scene>, resolution 2.50&Aring;
+<StructureSection load='1x9y' size='340' side='right'caption='[[1x9y]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<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>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-|GENE= sspB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
+<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>
-}}
+</table>
+== Function ==
+[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;">
+== 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.
-'''The prostaphopain B structure'''
+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<ref>PMID:15518582</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1x9y" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Proteinase 3D structures|Proteinase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-X9Y is a [[Single protein]] structure of sequence from [http://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].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-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:[http://www.ncbi.nlm.nih.gov/pubmed/15518582 15518582]
-[[Category: Single protein]]
 [[Category: Staphylococcus aureus]]
-[[Category: Bochtler, M.]]
+[[Category: Bochtler M]]
-[[Category: Filipek, R.]]
+[[Category: Filipek R]]
-[[Category: Potempa, J.]]
+[[Category: Potempa J]]
-[[Category: Sabat, A.]]
+[[Category: Sabat A]]
-[[Category: Szczepanowski, R.]]
+[[Category: Szczepanowski R]]
-[[Category: barrel-sandwich-hybrid]]
-[[Category: half-barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:06:59 2008''