1nyc: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1nyc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus Staphylococcus aureus subsp. aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NYC FirstGlance]. <br> | <table><tr><td colspan='2'>[[1nyc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus Staphylococcus aureus subsp. aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NYC FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">staphostatin B (sspC) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46170 Staphylococcus aureus subsp. aureus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">staphostatin B (sspC) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46170 Staphylococcus aureus subsp. aureus])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1nyc RCSB], [http://www.ebi.ac.uk/pdbsum/1nyc PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1nyc RCSB], [http://www.ebi.ac.uk/pdbsum/1nyc PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SSPC_STAAW SSPC_STAAW]] Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology (By similarity). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Staphylococcus aureus subsp. aureus]] | [[Category: Staphylococcus aureus subsp. aureus]] | ||
[[Category: Bochtler, M | [[Category: Bochtler, M]] | ||
[[Category: Dubin, A | [[Category: Dubin, A]] | ||
[[Category: Filipek, R | [[Category: Filipek, R]] | ||
[[Category: Kosowska, K | [[Category: Kosowska, K]] | ||
[[Category: Potempa, J | [[Category: Potempa, J]] | ||
[[Category: Rzychon, M | [[Category: Rzychon, M]] | ||
[[Category: Sabat, A | [[Category: Sabat, A]] | ||
[[Category: Cysteine protease inhibitor]] | [[Category: Cysteine protease inhibitor]] | ||
[[Category: Hydrolase inhibitor]] | [[Category: Hydrolase inhibitor]] | ||
[[Category: Sspc]] | [[Category: Sspc]] | ||
[[Category: Staphostatin b]] | [[Category: Staphostatin b]] | ||
Revision as of 03:27, 25 December 2014
Staphostatins resemble lipocalins, not cystatins in fold.Staphostatins resemble lipocalins, not cystatins in fold.
Structural highlights
Function[SSPC_STAAW] Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology (By similarity). Publication Abstract from PubMedStaphostatins 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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