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{{STRUCTURE_4gvp|  PDB=4gvp  |  SCENE=  }}
==Crystal Structure of the Response Regulator Protein VraR from Staphylococcus aureus==
===Crystal Structure of the Response Regulator Protein VraR from Staphylococcus aureus===
<StructureSection load='4gvp' size='340' side='right' caption='[[4gvp]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
{{ABSTRACT_PUBMED_23650349}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4gvp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_mu50 Staphylococcus aureus subsp. aureus mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GVP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GVP FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAV1884, vraR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 Staphylococcus aureus subsp. aureus Mu50])</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=4gvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gvp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gvp RCSB], [http://www.ebi.ac.uk/pdbsum/4gvp PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Staphylococcus aureus VraR, a vancomycin-resistance-associated response regulator, activates a cell-wall-stress stimulon in response to antibiotics that inhibit cell wall formation. X-ray crystal structures of VraR in both unphosphorylated and beryllofluoride-activated states have been determined, revealing a mechanism of phosphorylation-induced dimerization that features a deep hydrophobic pocket at the center of the receiver domain interface. Unphosphorylated VraR exists in a closed conformation that inhibits dimer formation. Phosphorylation at the active site promotes conformational changes that are propagated throughout the receiver domain, promoting the opening of a hydrophobic pocket that is essential for homodimer formation and enhanced DNA-binding activity. This prominent feature in the VraR dimer can potentially be exploited for the development of novel therapeutics to counteract antibiotic resistance in this important pathogen.


==About this Structure==
Phosphorylation-dependent conformational changes and domain rearrangements in Staphylococcus aureus VraR activation.,Leonard PG, Golemi-Kotra D, Stock AM Proc Natl Acad Sci U S A. 2013 May 21;110(21):8525-30. doi:, 10.1073/pnas.1302819110. Epub 2013 May 6. PMID:23650349<ref>PMID:23650349</ref>
[[4gvp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_mu50 Staphylococcus aureus subsp. aureus mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GVP OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:023650349</ref><references group="xtra"/><references/>
</div>
 
==See Also==
*[[Response regulator|Response regulator]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Staphylococcus aureus subsp. aureus mu50]]
[[Category: Staphylococcus aureus subsp. aureus mu50]]
[[Category: Leonard, P G.]]
[[Category: Leonard, P G]]
[[Category: Stock, A M.]]
[[Category: Stock, A M]]
[[Category: Bacterial signalling]]
[[Category: Bacterial signalling]]
[[Category: Dna binding]]
[[Category: Dna binding]]
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