View source for 5nla


==Crystal structure of the AraC-like transcriptional activator CuxR==
<StructureSection load='5nla' size='340' side='right'caption='[[5nla]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nla]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti_1021 Sinorhizobium meliloti 1021]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NLA 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]] 2.7&#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=5nla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nla OCA], [https://pdbe.org/5nla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nla RCSB], [https://www.ebi.ac.uk/pdbsum/5nla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nla ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q92WA5_RHIME Q92WA5_RHIME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cyclic dimeric GMP (c-di-GMP) has emerged as a key regulatory player in the transition between planktonic and sedentary biofilm-associated bacterial lifestyles. It controls a multitude of processes including production of extracellular polysaccharides (EPSs). The PilZ domain, consisting of an N-terminal "RxxxR" motif and a beta-barrel domain, represents a prototype c-di-GMP receptor. We identified a class of c-di-GMP-responsive proteins, represented by the AraC-like transcription factor CuxR in plant symbiotic alpha-proteobacteria. In Sinorhizobium meliloti, CuxR stimulates transcription of an EPS biosynthesis gene cluster at elevated c-di-GMP levels. CuxR consists of a Cupin domain, a helical hairpin, and bipartite helix-turn-helix motif. Although unrelated in sequence, the mode of c-di-GMP binding to CuxR is highly reminiscent to that of PilZ domains. c-di-GMP interacts with a conserved N-terminal RxxxR motif and the Cupin domain, thereby promoting CuxR dimerization and DNA binding. We unravel structure and mechanism of a previously unrecognized c-di-GMP-responsive transcription factor and provide insights into the molecular evolution of c-di-GMP binding to proteins.

AraC-like transcriptional activator CuxR binds c-di-GMP by a PilZ-like mechanism to regulate extracellular polysaccharide production.,Schaper S, Steinchen W, Krol E, Altegoer F, Skotnicka D, Sogaard-Andersen L, Bange G, Becker A Proc Natl Acad Sci U S A. 2017 Jun 13;114(24):E4822-E4831. doi:, 10.1073/pnas.1702435114. Epub 2017 May 30. PMID:28559336<ref>PMID:28559336</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nla" style="background-color:#fffaf0;"></div>

==See Also==
*[[Galectin 3D structures|Galectin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sinorhizobium meliloti 1021]]
[[Category: Altegoer F]]
[[Category: Bange G]]
[[Category: Steinchen WM]]