View source for 7dwo


==Crystal structure of Vibrio fischeri DarR in complex with DNA reveals the transcriptional activation mechanism of LTTR family members==
<StructureSection load='7dwo' size='340' side='right'caption='[[7dwo]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7dwo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliivibrio_fischeri_ES114 Aliivibrio fischeri ES114]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DWO 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]] 2.611&#8491;</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=7dwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dwo OCA], [https://pdbe.org/7dwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dwo RCSB], [https://www.ebi.ac.uk/pdbsum/7dwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dwo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5E4K6_ALIF1 Q5E4K6_ALIF1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DarR, a novel member of the LTTR family derived from Vibrio fischeri, activates transcription in response to d-Asp and regulates the overexpression of the racD genes encoding a putative aspartate racemase, RacD. Here, the crystal structure of full-length DarR and its mutant DarR-M202I were obtained by X-ray crystallography. According to the electron density map analysis of full-length DarR, the effector binding site of DarR is occupied by 2-Morpholinoethanesulfonic acid monohydrate (MES), which could interact with amino acids in the effector binding site and stabilize the effector binding site. Furthermore, we elaborated the structure of DarR-M202I, where methionine is replaced by isoleucine resulting in overexpression of the downstream operon. By comparing DarR-MES and DarR-M202I, we found similar behavior of DarR-MES in terms of the stability of the RD active pocket and the deflection angle of the DBD. The Isothermal titration calorimetry and Gel-filtration chromatography experiments showed that only when the target DNA sequence of a particular quasi-palindromic sequence exceeds 19bp, DarR can effectively bind to racD promoter. This study will help enhance our understanding of the mechanism in the transcriptional regulation of LTTR family transcription factors.

Crystal structure details of Vibrio fischeri DarR and mutant DarR-M202I from LTTR family reveals their activation mechanism.,Wang W, Wu H, Xiao Q, Zhou H, Li M, Xu Q, Wang Q, Yu F, He J Int J Biol Macromol. 2021 May 31;183:2354-2363. doi:, 10.1016/j.ijbiomac.2021.05.186. PMID:34081954<ref>PMID:34081954</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7dwo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aliivibrio fischeri ES114]]
[[Category: Large Structures]]
[[Category: He JH]]
[[Category: Wang WW]]
[[Category: Wu H]]
[[Category: Yu F]]