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== | ==Solution structure of staphostatin A form Staphylococcus aureus confirms the discovery of a novel class of cysteine proteinase inhibitors.== | ||
<StructureSection load='1oh1' size='340' side='right'caption='[[1oh1]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1oh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OH1 FirstGlance]. <br> | |||
</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=1oh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oh1 OCA], [https://pdbe.org/1oh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oh1 RCSB], [https://www.ebi.ac.uk/pdbsum/1oh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oh1 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A series of secreted proteases are included among the virulence factors documented for Staphylococcus aureus. In light of increasing antibiotic resistance of this dangerous human pathogen, these proteases are considered as suitable targets for the development of novel therapeutic strategies. The recent discovery of staphostatins, endogenous, highly specific, staphylococcal cysteine protease inhibitors, opened a possibility for structure-based design of low molecular weight analogues. Moreover, the crystal structure of staphostatin B revealed a distinct folding pattern and an unexpected, substrate-like binding mode. The solution structure of staphostatin A reported here confirms that staphostatins constitute a novel, distinct class of cysteine protease inhibitors. In addition, the structure knowledge-based mutagenesis studies shed light on individual structural features of staphostatin A, the inhibition mechanism, and the determinants of distinct specificity of staphostatins toward their target proteases. | A series of secreted proteases are included among the virulence factors documented for Staphylococcus aureus. In light of increasing antibiotic resistance of this dangerous human pathogen, these proteases are considered as suitable targets for the development of novel therapeutic strategies. The recent discovery of staphostatins, endogenous, highly specific, staphylococcal cysteine protease inhibitors, opened a possibility for structure-based design of low molecular weight analogues. Moreover, the crystal structure of staphostatin B revealed a distinct folding pattern and an unexpected, substrate-like binding mode. The solution structure of staphostatin A reported here confirms that staphostatins constitute a novel, distinct class of cysteine protease inhibitors. In addition, the structure knowledge-based mutagenesis studies shed light on individual structural features of staphostatin A, the inhibition mechanism, and the determinants of distinct specificity of staphostatins toward their target proteases. | ||
A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus.,Dubin G, Krajewski M, Popowicz G, Stec-Niemczyk J, Bochtler M, Potempa J, Dubin A, Holak TA Biochemistry. 2003 Nov 25;42(46):13449-56. PMID:14621990<ref>PMID:14621990</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1oh1" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Bochtler | [[Category: Bochtler M]] | ||
[[Category: Dubin | [[Category: Dubin A]] | ||
[[Category: Dubin | [[Category: Dubin G]] | ||
[[Category: Holak | [[Category: Holak TA]] | ||
[[Category: Krajewski | [[Category: Krajewski M]] | ||
[[Category: Popowicz | [[Category: Popowicz G]] | ||
[[Category: Potempa | [[Category: Potempa J]] | ||
[[Category: Stec | [[Category: Stec J]] | ||
Latest revision as of 13:51, 15 February 2023
Solution structure of staphostatin A form Staphylococcus aureus confirms the discovery of a novel class of cysteine proteinase inhibitors.Solution structure of staphostatin A form Staphylococcus aureus confirms the discovery of a novel class of cysteine proteinase inhibitors.
Structural highlights
Publication Abstract from PubMedA series of secreted proteases are included among the virulence factors documented for Staphylococcus aureus. In light of increasing antibiotic resistance of this dangerous human pathogen, these proteases are considered as suitable targets for the development of novel therapeutic strategies. The recent discovery of staphostatins, endogenous, highly specific, staphylococcal cysteine protease inhibitors, opened a possibility for structure-based design of low molecular weight analogues. Moreover, the crystal structure of staphostatin B revealed a distinct folding pattern and an unexpected, substrate-like binding mode. The solution structure of staphostatin A reported here confirms that staphostatins constitute a novel, distinct class of cysteine protease inhibitors. In addition, the structure knowledge-based mutagenesis studies shed light on individual structural features of staphostatin A, the inhibition mechanism, and the determinants of distinct specificity of staphostatins toward their target proteases. A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus.,Dubin G, Krajewski M, Popowicz G, Stec-Niemczyk J, Bochtler M, Potempa J, Dubin A, Holak TA Biochemistry. 2003 Nov 25;42(46):13449-56. PMID:14621990[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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