1oh1 | pdb_00001oh1

SOLUTION STRUCTURE OF STAPHOSTATIN A FORM STAPHYLOCOCCUS AUREUS CONFIRMS THE DISCOVERY OF A NOVEL CLASS OF CYSTEINE PROTEINASE INHIBITORS.

spinqualitylabelsall models 1oh1, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1oh1 is a 1 chain structure with sequence from Staphylococcus aureus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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