1nyc: Difference between revisions
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|PDB= 1nyc |SIZE=350|CAPTION= <scene name='initialview01'>1nyc</scene>, resolution 1.40Å | |PDB= 1nyc |SIZE=350|CAPTION= <scene name='initialview01'>1nyc</scene>, resolution 1.40Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= staphostatin B (sspC) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |GENE= staphostatin B (sspC) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyc OCA], [http://www.ebi.ac.uk/pdbsum/1nyc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nyc RCSB]</span> | |||
}} | }} | ||
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[[Category: Rzychon, M.]] | [[Category: Rzychon, M.]] | ||
[[Category: Sabat, A.]] | [[Category: Sabat, A.]] | ||
[[Category: cysteine protease inhibitor]] | [[Category: cysteine protease inhibitor]] | ||
[[Category: sspc]] | [[Category: sspc]] | ||
[[Category: staphostatin b]] | [[Category: staphostatin b]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:37:13 2008'' | ||
Revision as of 22:37, 30 March 2008
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| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | staphostatin B (sspC) (Staphylococcus aureus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Staphostatins resemble lipocalins, not cystatins in fold.
OverviewOverview
Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Here, we present the 1.4 A crystal structure of staphostatin B and show that the fold can be described as a fully closed, highly sheared eight-stranded beta-barrel. Thus, staphostatin B is related to beta-barrel domains that are involved in the inhibition or regulation of proteases of various catalytic types and to the superfamily of lipocalins/cytosolic fatty acid binding proteins. Unexpectedly for a cysteine protease inhibitor, staphostatin B is not significantly similar to cystatins.
About this StructureAbout this Structure
1NYC is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
Staphostatins resemble lipocalins, not cystatins in fold., Rzychon M, Filipek R, Sabat A, Kosowska K, Dubin A, Potempa J, Bochtler M, Protein Sci. 2003 Oct;12(10):2252-6. PMID:14500882
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