1Y4H

Wild type staphopain-staphostatin complex

Summary for 1Y4H

• Entry DOI: 10.2210/pdb1y4h/pdb
• Related: 1CV8 1NYC 1PXV 1X9Y
• Descriptor: cysteine protease, cysteine protease inhibitor, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: cysteine protease, inhibitor, staphopain b, staphostatin b, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Staphylococcus aureus; More
• Cellular location: Cytoplasm : Q9EYW6
• Total number of polymer chains: 4
• Total formula weight: 69584.35

Authors

Filipek, R.,Potempa, J.,Bochtler, M. (deposition date: 2004-11-30, release date: 2005-01-18, Last modification date: 2023-08-23)

Primary citation

Filipek, R.,Potempa, J.,Bochtler, M.
A comparison of staphostatin B with standard mechanism serine protease inhibitors.
J.Biol.Chem., 280:14669-14674, 2005

PubMed Abstract: Staphostatins are the endogenous, highly specific inhibitors of staphopains, the major secreted cysteine proteases from Staphylococcus aureus. We have previously shown that staphostatins A and B are competitive, active site-directed inhibitors that span the active site clefts of their target proteases in the same orientation as substrates. We now report the crystal structure of staphostatin B in complex with wild-type staphopain B at 1.9 A resolution. In the complex structure, the catalytic residues are found in exactly the positions that would be expected for uncomplexed papain-type proteases. There is robust, continuous density for the staphostatin B binding loop and no indication for cleavage of the peptide bond that comes closest to the active site cysteine of staphopain B. The carbonyl carbon atom C of this peptide bond is 4.1 A away from the active site cysteine sulfur Sgamma atom. The carbonyl oxygen atom O of this peptide bond points away from the putative oxyanion hole and lies almost on a line from the Sgamma atom to the C atom. The arrangement is strikingly similar to the "ionmolecule" arrangement for the complex of papain-type enzymes with their substrates but differs significantly from the arrangement conventionally assumed for the Michaelis complex of papain-type enzymes with their substrates and also from the arrangement that is crystallographically observed for complexes of standard mechanism inhibitors and their target serine proteases.

PubMed: 15644332
DOI: 10.1074/jbc.M411792200

Experimental method

X-RAY DIFFRACTION (1.93 Å)