1oh1
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SOLUTION STRUCTURE OF STAPHOSTATIN A FORM STAPHYLOCOCCUS AUREUS CONFIRMS THE DISCOVERY OF A NOVEL CLASS OF CYSTEINE PROTEINASE INHIBITORS.
OverviewOverview
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.
About this StructureAbout this Structure
1OH1 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
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
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