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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2kss]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KSS FirstGlance]. <br>
<table><tr><td colspan='2'>[[2kss]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus Myxococcus xanthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KSS 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=2kss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kss OCA], [https://pdbe.org/2kss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kss RCSB], [https://www.ebi.ac.uk/pdbsum/2kss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kss ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kss OCA], [https://pdbe.org/2kss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kss RCSB], [https://www.ebi.ac.uk/pdbsum/2kss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kss ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/CARS_MYXXA CARS_MYXXA] Involved in carotenoid biosynthesis. Antagonizes the transcriptional repressor proteins CarA and CarH by preventing their binding to DNA. Can also dissociate preformed CarA-DNA complexes. Does not bind DNA.<ref>PMID:11748235</ref> <ref>PMID:18315685</ref>  
[https://www.uniprot.org/uniprot/CARS_MYXXA CARS_MYXXA] Involved in carotenoid biosynthesis. Antagonizes the transcriptional repressor proteins CarA and CarH by preventing their binding to DNA. Can also dissociate preformed CarA-DNA complexes. Does not bind DNA.<ref>PMID:11748235</ref> <ref>PMID:18315685</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Direct targeting of critical DNA-binding elements of a repressor by its cognate antirepressor is an effective means to sequester the repressor and remove a transcription initiation block. Structural descriptions for this, though often proposed for bacterial and phage repressor-antirepressor systems, are unavailable. Here, we describe the structural and functional basis of how the Myxococcus xanthus CarS antirepressor recognizes and neutralizes its cognate repressors to turn on a photo-inducible promoter. CarA and CarH repress the carB operon in the dark. CarS, produced in the light, physically interacts with the MerR-type winged-helix DNA-binding domain of these repressors leading to activation of carB. The NMR structure of CarS1, a functional CarS variant, reveals a five-stranded, antiparallel beta-sheet fold resembling SH3 domains, protein-protein interaction modules prevalent in eukaryotes but rare in prokaryotes. NMR studies and analysis of site-directed mutants in vivo and in vitro unveil a solvent-exposed hydrophobic pocket lined by acidic residues in CarS, where the CarA DNA recognition helix docks with high affinity in an atypical ligand-recognition mode for SH3 domains. Our findings uncover an unprecedented use of the SH3 domain-like fold for protein-protein recognition whereby an antirepressor mimics operator DNA in sequestering the repressor DNA recognition helix to activate transcription.
A bacterial antirepressor with SH3 domain topology mimics operator DNA in sequestering the repressor DNA recognition helix.,Leon E, Navarro-Aviles G, Santiveri CM, Flores-Flores C, Rico M, Gonzalez C, Murillo FJ, Elias-Arnanz M, Jimenez MA, Padmanabhan S Nucleic Acids Res. 2010 Aug;38(15):5226-41. Epub 2010 Apr 21. PMID:20410074<ref>PMID:20410074</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kss" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 06:48, 1 May 2024

NMR structure of Myxococcus xanthus antirepressor CarS1

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