4q77
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4q77]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MRSA252 Staphylococcus aureus subsp. aureus MRSA252]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q77 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4q77]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MRSA252 Staphylococcus aureus subsp. aureus MRSA252]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q77 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 1.77Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=4q77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q77 OCA], [https://pdbe.org/4q77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q77 RCSB], [https://www.ebi.ac.uk/pdbsum/4q77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q77 ProSAT]</span></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=4q77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q77 OCA], [https://pdbe.org/4q77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q77 RCSB], [https://www.ebi.ac.uk/pdbsum/4q77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q77 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ROT_STAAR ROT_STAAR] Global regulator with both positive and negative effects that mediates modulation of several genes involved in virulence. Also, modulates the expression of genes not previously implicated in pathogenesis (By similarity). | [https://www.uniprot.org/uniprot/ROT_STAAR ROT_STAAR] Global regulator with both positive and negative effects that mediates modulation of several genes involved in virulence. Also, modulates the expression of genes not previously implicated in pathogenesis (By similarity). | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Staphylococcus aureus is a highly versatile pathogen that can infect human tissue by producing a large arsenal of virulence factors that are tightly regulated by a complex regulatory network. Rot, which shares sequence similarity with SarA homologues, is a global regulator that regulates numerous virulence genes. However, the recognition model of Rot for the promoter region of target genes and the putative regulation mechanism remain elusive. In this study, the 1.77 A resolution X-ray crystal structure of Rot is reported. The structure reveals that two Rot molecules form a compact homodimer, each of which contains a typical helix-turn-helix module and a beta-hairpin motif connected by a flexible loop. Fluorescence polarization results indicate that Rot preferentially recognizes AT-rich dsDNA with ~30-base-pair nucleotides and that the conserved positively charged residues on the winged-helix motif are vital for binding to the AT-rich dsDNA. It is proposed that the DNA-recognition model of Rot may be similar to that of SarA, SarR and SarS, in which the helix-turn-helix motifs of each monomer interact with the major grooves of target dsDNA and the winged motifs contact the minor grooves. Interestingly, the structure shows that Rot adopts a novel dimerization model that differs from that of other SarA homologues. As expected, perturbation of the dimer interface abolishes the dsDNA-binding ability of Rot, suggesting that Rot functions as a dimer. In addition, the results have been further confirmed in vivo by measuring the transcriptional regulation of alpha-toxin, a major virulence factor produced by most S. aureus strains. | ||
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| - | Structure of Rot, a global regulator of virulence genes in Staphylococcus aureus.,Zhu Y, Fan X, Zhang X, Jiang X, Niu L, Teng M, Li X Acta Crystallogr D Biol Crystallogr. 2014 Sep;70(Pt 9):2467-76. doi:, 10.1107/S1399004714015326. Epub 2014 Aug 29. PMID:25195759<ref>PMID:25195759</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4q77" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of Rot, a global regulator of virulence genes in Staphylococcus aureus
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