9ill
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==monomeric SarA-E89Q in complex with DNA== | |
+ | <StructureSection load='9ill' size='340' side='right'caption='[[9ill]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[9ill]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_N315 Staphylococcus aureus subsp. aureus N315] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ILL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9ILL FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=9ill FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ill OCA], [https://pdbe.org/9ill PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ill RCSB], [https://www.ebi.ac.uk/pdbsum/9ill PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ill ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/SARA_STAAN SARA_STAAN] Global regulator with both positive and negative effects that controls the expression of several virulence factors and the biofilm formation process in a cell density-dependent manner. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | SarA is a global transcription regulator in S. aureus which regulates the expression of over 120 genes related to quorum sensing, biofilm synthesis, drug resistance and many other important physiological processes during host infection. SarA can bind to the promoter region of agr and other target genes to activate or repress the transcription. The crystal structure of SarA uncovered a MarR protein-like conformation with two symmetrical winged helix domains, while its DNA binding mechanism is still unknown. We have constructed a monomeric DNA binding domain of SarA (SarA(DeltaN19)) for the study of the interaction between SarA and DNA with NMR spectroscopy. Here, we report the (1)H, (13)C and (15)N NMR assignment of SarA(DeltaN19)/DNA complex which is the first step towards further structure and function analysis. | ||
- | + | (1)H, (13)C, and (15)N resonance assignments of SarA monomer from Staphylococcus aureus in complex with DNA.,Fu D, Duan B, Dong X, Xia B Biomol NMR Assign. 2023 Dec;17(2):193-197. doi: 10.1007/s12104-023-10140-8. Epub , 2023 Jul 5. PMID:37405582<ref>PMID:37405582</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 9ill" style="background-color:#fffaf0;"></div> |
- | [[Category: Fu | + | == References == |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Staphylococcus aureus subsp. aureus N315]] | ||
+ | [[Category: Synthetic construct]] | ||
+ | [[Category: Fu DH]] | ||
+ | [[Category: Xia B]] |
Current revision
monomeric SarA-E89Q in complex with DNA
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