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[[Image:1nyc.jpg|left|200px]]<br /><applet load="1nyc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nyc, resolution 1.40&Aring;" />
'''Staphostatins resemble lipocalins, not cystatins in fold.'''<br />


==Overview==
==Staphostatins resemble lipocalins, not cystatins in fold.==
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.
<StructureSection load='1nyc' size='340' side='right'caption='[[1nyc]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
1NYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1NYC OCA].  
</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 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>
==Reference==
<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>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14500882 14500882]
</table>
[[Category: Single protein]]
== Function ==
[[Category: Staphylococcus aureus]]
[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).
[[Category: Bochtler, M.]]
__TOC__
[[Category: Dubin, A.]]
</StructureSection>
[[Category: Filipek, R.]]
[[Category: Large Structures]]
[[Category: Kosowska, K.]]
[[Category: Staphylococcus aureus subsp. aureus MW2]]
[[Category: Potempa, J.]]
[[Category: Bochtler M]]
[[Category: Rzychon, M.]]
[[Category: Dubin A]]
[[Category: Sabat, A.]]
[[Category: Filipek R]]
[[Category: CL]]
[[Category: Kosowska K]]
[[Category: SO4]]
[[Category: Potempa J]]
[[Category: cysteine protease inhibitor]]
[[Category: Rzychon M]]
[[Category: sspc]]
[[Category: Sabat A]]
[[Category: staphostatin b]]
 
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