View source for 4urq


==Crystal Structure of GGDEF domain (I site mutant) from T.maritima==
<StructureSection load='4urq' size='340' side='right'caption='[[4urq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4urq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4URQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4URQ 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]] 2.5&#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=4urq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4urq OCA], [https://pdbe.org/4urq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4urq RCSB], [https://www.ebi.ac.uk/pdbsum/4urq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4urq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9X2A8_THEMA Q9X2A8_THEMA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Large-scale production of bis-3'-5'-cyclic-di-GMP (c-di-GMP) would facilitate biological studies of numerous bacterial signaling pathways and phenotypes controlled by this second messenger molecule, such as virulence and biofilm formation. C-di-GMP constitutes also a potentially interesting molecule as a vaccine adjuvant. Even though chemical synthesis of c-di-GMP can be done, the yields are incompatible with mass-production. tDGC, a stand-alone diguanylate cyclase (DGC or GGDEF domain) from Thermotoga maritima, enables the robust enzymatic production of large quantities of c-di-GMP. To understand the structural correlates of tDGC thermostability, its catalytic mechanism and feedback inhibition, we determined structures of an active-like dimeric conformation with both active (A) sites facing each other and of an inactive dimeric conformation, locked by c-di-GMP bound at the inhibitory (I) site. We also report the structure of a single mutant of tDGC, with the R158A mutation at the I-site, abolishing product inhibition and unproductive dimerization. A comparison with structurally characterized DGC homologues from mesophiles reveals the presence of a higher number of salt bridges in the hyperthermophile enzyme tDGC. Denaturation experiments of mutants disrupting in turn each of the salt bridges unique to tDGC identified three salt-bridges critical to confer thermostability.

Structure of a Diguanylate Cyclase from Thermotoga maritima: Insights into Activation, Feedback Inhibition and Thermostability.,Deepthi A, Liew CW, Liang ZX, Swaminathan K, Lescar J PLoS One. 2014 Oct 31;9(10):e110912. doi: 10.1371/journal.pone.0110912., eCollection 2014. PMID:25360685<ref>PMID:25360685</ref>

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

==See Also==
*[[Diguanylate cyclase|Diguanylate cyclase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Deepthi A]]
[[Category: Lescar J]]
[[Category: Liang ZX]]
[[Category: Liew CW]]
[[Category: Swamianthan K]]