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| - | [[Image:1y4h.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1y4h.png|left|200px]] |
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| | {{STRUCTURE_1y4h| PDB=1y4h | SCENE= }} | | {{STRUCTURE_1y4h| PDB=1y4h | SCENE= }} |
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| - | '''Wild type staphopain-staphostatin complex'''
| + | ===Wild type staphopain-staphostatin complex=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15644332}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15644332 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15644332}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Staphopain b]] | | [[Category: Staphopain b]] |
| | [[Category: Staphostatin b]] | | [[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 Mon Jul 28 19:12:24 2008'' |
Revision as of 16:12, 28 July 2008
Template:STRUCTURE 1y4h
Wild type staphopain-staphostatin complex
Template:ABSTRACT PUBMED 15644332
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 Mon Jul 28 19:12:24 2008
