1nyc: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Staphostatins resemble lipocalins, not cystatins in fold.==
-<StructureSection load='1nyc' size='340' side='right' caption='[[1nyc]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+<StructureSection load='1nyc' size='340' side='right'caption='[[1nyc]], [[Resolution|resolution]] 1.40&Aring;' 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>
+<table><tr><td colspan='2'>[[1nyc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MW2 Staphylococcus aureus subsp. aureus MW2]. 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 [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1nyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyc OCA], [https://pdbe.org/1nyc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nyc RCSB], [https://www.ebi.ac.uk/pdbsum/1nyc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nyc ProSAT]</span></td></tr>
-<table>
+</table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://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).
-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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Staphylococcus aureus subsp. aureus]]
+[[Category: Large Structures]]
-[[Category: Bochtler, M.]]
+[[Category: Staphylococcus aureus subsp. aureus MW2]]
-[[Category: Dubin, A.]]
+[[Category: Bochtler M]]
-[[Category: Filipek, R.]]
+[[Category: Dubin A]]
-[[Category: Kosowska, K.]]
+[[Category: Filipek R]]
-[[Category: Potempa, J.]]
+[[Category: Kosowska K]]
-[[Category: Rzychon, M.]]
+[[Category: Potempa J]]
-[[Category: Sabat, A.]]
+[[Category: Rzychon M]]
-[[Category: Cysteine protease inhibitor]]
+[[Category: Sabat A]]
-[[Category: Hydrolase inhibitor]]
-[[Category: Sspc]]
-[[Category: Staphostatin b]]