6e52

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Current revision (14:39, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6e52' size='340' side='right'caption='[[6e52]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
<StructureSection load='6e52' size='340' side='right'caption='[[6e52]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6e52]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E52 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6e52]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Z172 Staphylococcus aureus subsp. aureus Z172]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E52 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">agrC, SAZ172_2038 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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]] 1.93&#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=6e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e52 OCA], [http://pdbe.org/6e52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e52 RCSB], [http://www.ebi.ac.uk/pdbsum/6e52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e52 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=6e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e52 OCA], [https://pdbe.org/6e52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e52 RCSB], [https://www.ebi.ac.uk/pdbsum/6e52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e52 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST]] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.
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[https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Virulence induction in the Staphylococcus aureus is under the control of a quorum sensing (QS) circuit encoded by the accessory gene regulator (agr) locus. Allelic variation within agr produces four QS specificity groups, each producing a unique secreted autoinducer peptide (AIP) and receptor histidine kinase (RHK), AgrC. Cognate AIP-AgrC interactions activate virulence through a two-component signaling cascade, whereas non-cognate pairs are generally inhibitory. Here we pinpoint a key hydrogen-bonding interaction within AgrC that acts as a switch to convert helical motions propagating from the receptor sensor domain into changes in inter-domain association within the kinase module. AgrC mutants lacking this interaction are constitutively active in vitro and in vivo, the latter leading to a pronounced attenuation of S. aureus biofilm formation. Thus, our work sheds light on the regulation of this biomedically important RHK.
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Identification of a Molecular Latch that Regulates Staphylococcal Virulence.,Xie Q, Zhao A, Jeffrey PD, Kim MK, Bassler BL, Stone HA, Novick RP, Muir TW Cell Chem Biol. 2019 Jan 31. pii: S2451-9456(19)30028-5. doi:, 10.1016/j.chembiol.2019.01.006. PMID:30773482<ref>PMID:30773482</ref>
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==See Also==
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*[[Gcn4 3D Structures|Gcn4 3D Structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Gnc4 3D Structures|Gnc4 3D Structures]]
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</div>
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<div class="pdbe-citations 6e52" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jeffrey, P D]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Muir, T W]]
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[[Category: Staphylococcus aureus subsp. aureus Z172]]
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[[Category: Xie, Q]]
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[[Category: Jeffrey PD]]
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[[Category: Bacterial quorum sensing]]
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[[Category: Muir TW]]
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[[Category: Bergerat fold]]
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[[Category: Xie Q]]
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[[Category: Coiled coil]]
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[[Category: Protein histidine kinase]]
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[[Category: Signaling protein]]
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Current revision

Chimeric structure of Saccharomyces cerevisiae GCN4 leucine zipper fused to Staphylococcus aureus AgrC cytoplasmic histidine kinase module (dataset anisotropically truncated by STARANISO)

PDB ID 6e52

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