4wu4: Difference between revisions
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==Crystal structure of E. faecalis DNA binding domain LiaRD191N complexed with 22bp DNA== | ==Crystal structure of E. faecalis DNA binding domain LiaRD191N complexed with 22bp DNA== | ||
<StructureSection load='4wu4' size='340' side='right' caption='[[4wu4]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4wu4' size='340' side='right'caption='[[4wu4]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wu4]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4wu4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis_S613 Enterococcus faecalis S613]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WU4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wu4 OCA], [https://pdbe.org/4wu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wu4 RCSB], [https://www.ebi.ac.uk/pdbsum/4wu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wu4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 17: | Line 17: | ||
</div> | </div> | ||
<div class="pdbe-citations 4wu4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4wu4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Response regulator 3D structure|Response regulator 3D structure]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Enterococcus faecalis | [[Category: Enterococcus faecalis S613]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Davlieva M]] | ||
[[Category: | [[Category: Shamoo Y]] | ||
Latest revision as of 03:55, 28 December 2023
Crystal structure of E. faecalis DNA binding domain LiaRD191N complexed with 22bp DNACrystal structure of E. faecalis DNA binding domain LiaRD191N complexed with 22bp DNA
Structural highlights
Publication Abstract from PubMedLiaR is a 'master regulator' of the cell envelope stress response in enterococci and many other Gram-positive organisms. Mutations to liaR can lead to antibiotic resistance to a variety of antibiotics including the cyclic lipopeptide daptomycin. LiaR is phosphorylated in response to membrane stress to regulate downstream target operons. Using DNA footprinting of the regions upstream of the liaXYZ and liaFSR operons we show that LiaR binds an extended stretch of DNA that extends beyond the proposed canonical consensus sequence suggesting a more complex level of regulatory control of target operons. We go on to determine the biochemical and structural basis for increased resistance to daptomycin by the adaptive mutation to LiaR (D191N) first identified from the pathogen Enterococcus faecalis S613. LiaRD191N increases oligomerization of LiaR to form a constitutively activated tetramer that has high affinity for DNA even in the absence of phosphorylation leading to increased resistance. Crystal structures of the LiaR DNA binding domain complexed to the putative consensus sequence as well as an adjoining secondary sequence show that upon binding, LiaR induces DNA bending that is consistent with increased recruitment of RNA polymerase to the transcription start site and upregulation of target operons. A variable DNA recognition site organization establishes the LiaR-mediated cell envelope stress response of enterococci to daptomycin.,Davlieva M, Shi Y, Leonard PG, Johnson TA, Zianni MR, Arias CA, Ladbury JE, Shamoo Y Nucleic Acids Res. 2015 Apr 19. pii: gkv321. PMID:25897118[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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