View source for 4zzd


==CRYSTAL STRUCTURE OF MULTIDRUG RESISTANCE REGULATOR LMRR BOUND TO RIBOFLAVIN==
<StructureSection load='4zzd' size='340' side='right'caption='[[4zzd]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zzd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._cremoris_MG1363 Lactococcus lactis subsp. cremoris MG1363]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZZD 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]] 2.351&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</scene></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=4zzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zzd OCA], [https://pdbe.org/4zzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zzd RCSB], [https://www.ebi.ac.uk/pdbsum/4zzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zzd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2RI36_LACLM A2RI36_LACLM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The heterodimeric ABC transporter LmrCD from Lactococcus lactis is able to extrude several different toxic compounds from the cell, fulfilling a role in the intrinsic and induced drug resistance. The expression of the lmrCD genes is regulated by the multi-drug binding repressor LmrR, which also binds to its own promoter to autoregulate its own expression. Previously, we reported the crystal structure of LmrR in the presence and absence of the drugs Hoechst 33342 and daunomycin. Analysis of the mechanism how drugs control the repressor activity of LmrR is impeded by the fact that these drugs also bind to DNA. Here we identified, using X-ray crystallography and fluorescence, that riboflavin binds into the drug binding cavity of LmrR, adopting a similar binding mode as Hoechst 33342 and daunomycin. Microscale thermophoresis was employed to quantify the binding affinity of LmrR to its responsive promoter regions and to evaluate the cognate site of LmrR in the lmrCD promoter region. Riboflavin reduces the binding affinity of LmrR for the promoter regions. Our results support a model wherein drug binding to LmrR relieves the LmrR dependent repression of the lmrCD genes.

Binding of the Lactococcal Drug Dependent Transcriptional Regulator LmrR to Its Ligands and Responsive Promoter Regions.,van der Berg JP, Madoori PK, Komarudin AG, Thunnissen AM, Driessen AJ PLoS One. 2015 Aug 12;10(8):e0135467. doi: 10.1371/journal.pone.0135467., eCollection 2015. PMID:26267906<ref>PMID:26267906</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zzd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Lactococcus lactis subsp. cremoris MG1363]]
[[Category: Large Structures]]
[[Category: Madoori PK]]
[[Category: Thunnissen A-MWH]]