4gvp

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==Crystal Structure of the Response Regulator Protein VraR from Staphylococcus aureus==
==Crystal Structure of the Response Regulator Protein VraR from Staphylococcus aureus==
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<StructureSection load='4gvp' size='340' side='right' caption='[[4gvp]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
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<StructureSection load='4gvp' size='340' side='right'caption='[[4gvp]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gvp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. 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>
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<table><tr><td colspan='2'>[[4gvp]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4GVP FirstGlance]. <br>
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</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 STAAM])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03&#8491;</td></tr>
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<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://pdbe.org/4gvp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gvp RCSB], [http://www.ebi.ac.uk/pdbsum/4gvp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gvp ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gvp OCA], [https://pdbe.org/4gvp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gvp RCSB], [https://www.ebi.ac.uk/pdbsum/4gvp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gvp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VRAR_STAAM VRAR_STAAM]] Member of the two-component regulatory system VraS/VraR involved in the control of the cell wall peptidoglycan biosynthesis. VraR is overexpressed in strain Mu50, which leads to vancomycin resistance.
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[https://www.uniprot.org/uniprot/VRAR_STAAM VRAR_STAAM] Member of the two-component regulatory system VraS/VraR involved in the control of the cell wall peptidoglycan biosynthesis. VraR is overexpressed in strain Mu50, which leads to vancomycin resistance.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4gvp" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Response regulator|Response regulator]]
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*[[Response regulator 3D structure|Response regulator 3D structure]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Staam]]
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[[Category: Large Structures]]
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[[Category: Leonard, P G]]
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[[Category: Staphylococcus aureus subsp. aureus Mu50]]
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[[Category: Stock, A M]]
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[[Category: Leonard PG]]
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[[Category: Bacterial signalling]]
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[[Category: Stock AM]]
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[[Category: Dna binding]]
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[[Category: Response regulator]]
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[[Category: Transcription]]
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[[Category: Transcription factor]]
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[[Category: Two-component system]]
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Current revision

Crystal Structure of the Response Regulator Protein VraR from Staphylococcus aureus

PDB ID 4gvp

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