4hqe: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4hqe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HQE FirstGlance]. <br>
-</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=4hqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hqe OCA], [https://pdbe.org/4hqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hqe RCSB], [https://www.ebi.ac.uk/pdbsum/4hqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hqe ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.299&#8491;</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=4hqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hqe OCA], [https://pdbe.org/4hqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hqe RCSB], [https://www.ebi.ac.uk/pdbsum/4hqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hqe ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/A0A0H3JWI0_STAAM A0A0H3JWI0_STAAM]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Quinone molecules are intracellular electron-transport carriers, as well as critical intra- and extracellular signals. However, transcriptional regulation of quinone signaling and its molecular basis are poorly understood. Here, we identify a thiol-stress-sensing regulator YodB family transcriptional regulator as a central component of quinone stress response of Staphylococcus aureus, which we have termed the quinone-sensing and response repressor (QsrR). We also identify and confirm an unprecedented quinone-sensing mechanism based on the S-quinonization of the essential residue Cys-5. Structural characterizations of the QsrR-DNA and QsrR-menadione complexes further reveal that the covalent association of menadione directly leads to the release of QsrR from operator DNA following a 10 degrees rigid-body rotation as well as a 9-A elongation between the dimeric subunits. The molecular level characterization of this quinone-sensing transcriptional regulator provides critical insights into quinone-mediated gene regulation in human pathogens.
-Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR.,Ji Q, Zhang L, Jones MB, Sun F, Deng X, Liang H, Cho H, Brugarolas P, Gao YN, Peterson SN, Lan L, Bae T, He C Proc Natl Acad Sci U S A. 2013 Mar 26;110(13):5010-5. doi:, 10.1073/pnas.1219446110. Epub 2013 Mar 11. PMID:23479646<ref>PMID:23479646</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4hqe" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>