4urq: Difference between revisions

Line 6:

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4urq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4urq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4urq RCSB], [http://www.ebi.ac.uk/pdbsum/4urq PDBsum]</span></td></tr>

</table>

== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Deepthi, A.]]

[[Category: Deepthi, A]]

[[Category: Lescar, J.]]

[[Category: Lescar, J]]

[[Category: Liang, Z X.]]

[[Category: Liang, Z X]]

[[Category: Liew, C W.]]

[[Category: Liew, C W]]

[[Category: Swamianthan, K.]]

[[Category: Swamianthan, K]]

[[Category: Transferase]]

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@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4urq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4urq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4urq RCSB], [http://www.ebi.ac.uk/pdbsum/4urq PDBsum]</span></td></tr>
 </table>
+<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>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Deepthi, A.]]
+[[Category: Deepthi, A]]
-[[Category: Lescar, J.]]
+[[Category: Lescar, J]]
-[[Category: Liang, Z X.]]
+[[Category: Liang, Z X]]
-[[Category: Liew, C W.]]
+[[Category: Liew, C W]]
-[[Category: Swamianthan, K.]]
+[[Category: Swamianthan, K]]
 [[Category: Transferase]]