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[[Image:1pxv.jpg|left|200px]]


{{Structure
==The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease==
|PDB= 1pxv |SIZE=350|CAPTION= <scene name='initialview01'>1pxv</scene>, resolution 1.80&Aring;
<StructureSection load='1pxv' size='340' side='right'caption='[[1pxv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1pxv]] 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=1PXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXV 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]] 1.8&#8491;</td></tr>
|GENE= staphopain B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]), staphostatin B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxv OCA], [https://pdbe.org/1pxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxv RCSB], [https://www.ebi.ac.uk/pdbsum/1pxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxv ProSAT]</span></td></tr>
|RELATEDENTRY=[[1nyc|1NYC]], [[1cv8|1CV8]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxv OCA], [http://www.ebi.ac.uk/pdbsum/1pxv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pxv RCSB]</span>
== 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 ==
Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Our recent crystal structure of staphostatin B has shown that this inhibitor forms a mixed, eight-stranded beta-barrel with statistically significant similarity to lipocalins, but not to cystatins. We now present the 1.8-A crystal structure of staphostatin B in complex with an inactive mutant of its target protease. The complex is held together through extensive interactions and buries a total surface area of 2300 A2. Unexpectedly for a cysteine protease inhibitor, staphostatin B binds to staphopain B in an almost substrate-like manner. The inhibitor polypeptide chain runs through the protease active site cleft in the forward direction, with residues IG-TS in P2 to P2' positions. Both in the free and complexed forms, the P1 glycine residue of the inhibitor is in a main chain conformation only accessible to glycines. Mutations in this residue lead to a loss of affinity of the inhibitor for protease and convert the inhibitor into a substrate.


'''The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease'''
The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease.,Filipek R, Rzychon M, Oleksy A, Gruca M, Dubin A, Potempa J, Bochtler M J Biol Chem. 2003 Oct 17;278(42):40959-66. Epub 2003 Jul 21. PMID:12874290<ref>PMID:12874290</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pxv" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Our recent crystal structure of staphostatin B has shown that this inhibitor forms a mixed, eight-stranded beta-barrel with statistically significant similarity to lipocalins, but not to cystatins. We now present the 1.8-A crystal structure of staphostatin B in complex with an inactive mutant of its target protease. The complex is held together through extensive interactions and buries a total surface area of 2300 A2. Unexpectedly for a cysteine protease inhibitor, staphostatin B binds to staphopain B in an almost substrate-like manner. The inhibitor polypeptide chain runs through the protease active site cleft in the forward direction, with residues IG-TS in P2 to P2' positions. Both in the free and complexed forms, the P1 glycine residue of the inhibitor is in a main chain conformation only accessible to glycines. Mutations in this residue lead to a loss of affinity of the inhibitor for protease and convert the inhibitor into a substrate.
*[[Proteinase 3D structures|Proteinase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1PXV is a [[Protein complex]] structure of sequences 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=1PXV OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease., Filipek R, Rzychon M, Oleksy A, Gruca M, Dubin A, Potempa J, Bochtler M, J Biol Chem. 2003 Oct 17;278(42):40959-66. Epub 2003 Jul 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12874290 12874290]
[[Category: Protein complex]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Bochtler, M.]]
[[Category: Bochtler M]]
[[Category: Dubin, A.]]
[[Category: Dubin A]]
[[Category: Filipek, R.]]
[[Category: Filipek R]]
[[Category: Gruca, M.]]
[[Category: Gruca M]]
[[Category: Oleksy, A.]]
[[Category: Oleksy A]]
[[Category: Potempa, J.]]
[[Category: Potempa J]]
[[Category: Rzychon, M.]]
[[Category: Rzychon M]]
[[Category: cysteine protease inhibitor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:06:02 2008''

Latest revision as of 11:24, 2 August 2023

The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease

1pxv, resolution 1.80Å

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