8sva
From Proteopedia
(Difference between revisions)
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<StructureSection load='8sva' size='340' side='right'caption='[[8sva]], [[Resolution|resolution]] 2.96Å' scene=''> | <StructureSection load='8sva' size='340' side='right'caption='[[8sva]], [[Resolution|resolution]] 2.96Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[8sva]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus Rhodococcus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SVA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[8sva]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus Rhodococcus] and [https://en.wikipedia.org/wiki/Rhodococcus_sp._USK13 Rhodococcus sp. USK13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SVA FirstGlance]. <br> |
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.96Å</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]] 2.96Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0A2S8J6Y8_RHOOP A0A2S8J6Y8_RHOOP] | [https://www.uniprot.org/uniprot/A0A2S8J6Y8_RHOOP A0A2S8J6Y8_RHOOP] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The mycobacterial repressor, DarR, a TetR family regulator (TFR), was the first transcription regulator shown to bind c-di-AMP. However, the molecular basis for this interaction and the mechanism involved in DNA binding by DarR remain unknown. Here we describe DarR-c-di-AMP and DarR-DNA structures and complementary biochemical assays. The DarR-c-di-AMP structure reveals a unique effector binding site for a TFR, located between DarR dimer subunits. Strikingly, we show this motif also binds cAMP. The location of the adenine nucleotide binding site between subunits suggests this interaction may facilitate dimerization and hence DNA binding. Indeed, biochemical assays show cAMP enhances DarR DNA binding. Finally, DarR-DNA structures reveal a distinct TFR DNA-binding mechanism involving two interacting dimers on the DNA. Thus, the combined data unveil a newly described second messenger binding motif and DNA binding mode for this important family of regulators. | ||
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| + | Structures of the DarR transcription regulator reveal unique modes of second messenger and DNA binding.,Schumacher MA, Lent N, Chen VB, Salinas R Nat Commun. 2023 Nov 9;14(1):7239. doi: 10.1038/s41467-023-42823-0. PMID:37945601<ref>PMID:37945601</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8sva" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Rhodococcus]] | [[Category: Rhodococcus]] | ||
| + | [[Category: Rhodococcus sp. USK13]] | ||
[[Category: Schumacher MA]] | [[Category: Schumacher MA]] | ||
Current revision
Structure of the Rhodococcus sp. USK13 DarR-20 bp DNA complex
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