1y4h
From Proteopedia
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[[Image:1y4h.gif|left|200px]] | [[Image:1y4h.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1y4h| PDB=1y4h | SCENE= }} | |
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'''Wild type staphopain-staphostatin complex''' | '''Wild type staphopain-staphostatin complex''' | ||
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[[Category: Filipek, R.]] | [[Category: Filipek, R.]] | ||
[[Category: Potempa, J.]] | [[Category: Potempa, J.]] | ||
| - | [[Category: | + | [[Category: Cysteine protease]] |
| - | [[Category: | + | [[Category: Inhibitor]] |
| - | [[Category: | + | [[Category: Staphopain b]] |
| - | [[Category: | + | [[Category: Staphostatin b]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:52:02 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:52, 3 May 2008
Wild type staphopain-staphostatin complex
Overview
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.
About this Structure
1Y4H is a Protein complex structure of sequences from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
A comparison of staphostatin B with standard mechanism serine protease inhibitors., Filipek R, Potempa J, Bochtler M, J Biol Chem. 2005 Apr 15;280(15):14669-74. Epub 2005 Jan 11. PMID:15644332 Page seeded by OCA on Sat May 3 15:52:02 2008
