1y4h: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1y4h.gif|left|200px]] | [[Image:1y4h.gif|left|200px]] | ||
'''Wild type staphopain-staphostatin complex''' | {{Structure | ||
|PDB= 1y4h |SIZE=350|CAPTION= <scene name='initialview01'>1y4h</scene>, resolution 1.93Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= sspB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]), sspC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |||
}} | |||
'''Wild type staphopain-staphostatin complex''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1Y4H is a [ | 1Y4H is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y4H OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15644332 15644332] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
| Line 23: | Line 32: | ||
[[Category: staphostatin b]] | [[Category: staphostatin b]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:18:21 2008'' | ||
Revision as of 13:18, 20 March 2008
| |||||||||||||
| 1y4h, resolution 1.93Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | CL and SO4 | ||||||||||||
| Gene: | sspB (Staphylococcus aureus), sspC (Staphylococcus aureus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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 Thu Mar 20 15:18:21 2008
