1nyc
From Proteopedia
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| - | [[ | + | ==Staphostatins resemble lipocalins, not cystatins in fold.== |
| + | <StructureSection load='1nyc' size='340' side='right' caption='[[1nyc]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == 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> | ||
| + | </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><br> | ||
| + | <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><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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:14500882</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Staphylococcus aureus subsp. aureus]] | [[Category: Staphylococcus aureus subsp. aureus]] | ||
[[Category: Bochtler, M.]] | [[Category: Bochtler, M.]] | ||
Revision as of 15:19, 28 September 2014
Staphostatins resemble lipocalins, not cystatins in fold.
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