1y4h

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[[Image:1y4h.gif|left|200px]]<br /><applet load="1y4h" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1y4h.gif|left|200px]]
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caption="1y4h, resolution 1.93&Aring;" />
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'''Wild type staphopain-staphostatin complex'''<br />
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{{Structure
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|PDB= 1y4h |SIZE=350|CAPTION= <scene name='initialview01'>1y4h</scene>, resolution 1.93&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY=
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|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])
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}}
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'''Wild type staphopain-staphostatin complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Y4H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y4H OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15644332 15644332]
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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]]
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[[Category: staphostatin b]]
[[Category: staphostatin b]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:40 2008''
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''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


PDB ID 1y4h

Drag the structure with the mouse to rotate
, resolution 1.93Å
Ligands: and
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

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