4xxe: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4xxe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL] 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=4XXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XXE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4xxe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL] 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=4XXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XXE 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=4xxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xxe OCA], [https://pdbe.org/4xxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xxe RCSB], [https://www.ebi.ac.uk/pdbsum/4xxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xxe 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]] 3.2&#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=4xxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xxe OCA], [https://pdbe.org/4xxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xxe RCSB], [https://www.ebi.ac.uk/pdbsum/4xxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xxe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/AGRA_STAAC AGRA_STAAC] Required for high-level post-exponential phase expression of a series of secreted proteins.
[https://www.uniprot.org/uniprot/AGRA_STAAC AGRA_STAAC] Required for high-level post-exponential phase expression of a series of secreted proteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The intracellular trigger for the quorum sensing response mechanism in Staphylococcus aureus involves the phosphorylation of the response regulator AgrA by the membrane anchored histidine kinase AgrC. AgrA activates transcription from three promoter sequences (P1-P3). The promoter strength, conditional association of AgrA with these promoter elements and temporal delay in AgrA-mediated changes in gene expression contribute to the diversity of the quorum sensing response in different S. aureus strains. AgrA promoters comprise of imperfect direct repeats of DNA with a consensus sequence- [TA][AC][CA]GTTN[AG][TG]. Here we describe crystal structures of the DNA-binding (LytTR) domain of AgrA with different cognate DNA sequences that reveal a hitherto unanticipated feature of AgrA-DNA interactions. AgrA promoter interactions are asymmetric with fewer interactions at the binding site proximal to the -35 promoter element. Biochemical assays to evaluate AgrA-promoter interactions suggests that phosphorylation induced dimerization of AgrA can compensate for the asymmetry in AgrA-DNA interactions. The structures also provide a basis to rationalize mutations that were noted to alter AgrA activity without affecting protein-DNA interactions. Put together, the structural data, gene expression and mutational analysis reveal that promoter strength and AgrA phosphorylation enable quorum-sensing triggered transcriptional changes leading to a transition from the persistent to virulent phenotype.
Conformational features of the Staphylococcus aureus AgrA-promoter interactions rationalize quorum-sensing triggered gene expression.,Rajasree K, Fasim A, Gopal B Biochem Biophys Rep. 2016 Mar 23;6:124-134. doi: 10.1016/j.bbrep.2016.03.012., eCollection 2016 Jul. PMID:28955870<ref>PMID:28955870</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4xxe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 09:02, 20 March 2024

Structure of AgrA LytTR domain in complex with promoters

4xxe, resolution 3.20Å

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