4gvp
From Proteopedia
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| - | + | ==Crystal Structure of the Response Regulator Protein VraR from Staphylococcus aureus== | |
| - | + | <StructureSection load='4gvp' size='340' side='right' caption='[[4gvp]], [[Resolution|resolution]] 2.03Å' scene=''> | |
| - | + | == 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. | ||
| - | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </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]] | ||
Revision as of 10:57, 21 December 2014
Crystal Structure of the Response Regulator Protein VraR from Staphylococcus aureus
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