6c29: Difference between revisions

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-'''Unreleased structure'''
-The entry 6c29 is ON HOLD  until Paper Publication
+==Crystal structure of the N-terminal periplasmic domain of ScsB from Proteus mirabilis==
+<StructureSection load='6c29' size='340' side='right'caption='[[6c29]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6c29]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Promh Promh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C29 FirstGlance]. <br>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMI0439 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=529507 PROMH])</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=6c29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c29 OCA], [http://pdbe.org/6c29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c29 RCSB], [http://www.ebi.ac.uk/pdbsum/6c29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c29 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Correct disulfide bond formation is essential for proper folding of many proteins, including bacterial virulence factors. The suppressor of copper sensitivity (Scs) proteins have roles in dithiol/disulfide interchange and the bacterial response to copper stress. Encoded in a four-gene cassette (ScsABCD) present in many Gram-negative bacteria, the Scs proteins are enigmatic and poorly characterised. Here, we show that the periplasmic alpha domain of the membrane protein ScsB in the Gram-negative bacterium Proteus mirabilis forms a redox relay with the soluble periplasmic protein PmScsC. We also found that the periplasmic alpha domain is sufficient to activate the disulfide isomerase activity of PmScsC. The crystal structure of PmScsBalpha at a resolution of 1.54 A revealed that it comprises two structurally similar immunoglobulin-like folds, one of which includes a putative redox-active site with the sequence CXXXC. We confirmed the importance of these cysteine residues for PmScsBalpha function and engineered cysteine variants that produced a stable complex between PmScsC and PmScsBalpha. Using small-angle X-ray and neutron scattering analyses with contrast variation, we determined a low-resolution structure of the PmScsC-PmScsBalpha complex. The structural model of this complex suggested that PmScsBalpha uses both of its immunoglobulin-like folds to interact with PmScsC and also revealed that the highly dynamic PmScsC becomes ordered upon PmScsBalpha binding. These findings add to our understanding of the poorly characterised Scs proteins.
-Authors: Furlong, E.J., Choudhury, H.G., Kurth, F., Martin, J.L.
+Disulfide isomerase activity of the dynamic, trimeric Proteus mirabilis ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.,Furlong EJ, Choudhury HG, Kurth F, Duff AP, Whitten AE, Martin JL J Biol Chem. 2018 Feb 28. pii: RA118.001860. doi: 10.1074/jbc.RA118.001860. PMID:29491145<ref>PMID:29491145</ref>
-Description: Crystal structure of the N-terminal periplasmic domain of ScsB from Proteus mirabilis
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Martin, J.L]]
+<div class="pdbe-citations 6c29" style="background-color:#fffaf0;"></div>
-[[Category: Furlong, E.J]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Promh]]
+[[Category: Choudhury, H G]]
+[[Category: Furlong, E J]]
 [[Category: Kurth, F]]
-[[Category: Choudhury, H.G]]
+[[Category: Martin, J L]]
+[[Category: Cysteine active site]]
+[[Category: Immunoglobulin fold]]
+[[Category: Oxidoreductase]]
+[[Category: Redox enzyme]]