4urq: Difference between revisions
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<StructureSection load='4urq' size='340' side='right'caption='[[4urq]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4urq' size='340' side='right'caption='[[4urq]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4urq]] is a 6 chain structure with sequence from [ | <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> | </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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9X2A8_THEMA Q9X2A8_THEMA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Deepthi | [[Category: Thermotoga maritima]] | ||
[[Category: Lescar | [[Category: Deepthi A]] | ||
[[Category: Liang | [[Category: Lescar J]] | ||
[[Category: Liew | [[Category: Liang ZX]] | ||
[[Category: Swamianthan | [[Category: Liew CW]] | ||
[[Category: Swamianthan K]] | |||
Revision as of 10:34, 29 March 2023
Crystal Structure of GGDEF domain (I site mutant) from T.maritimaCrystal Structure of GGDEF domain (I site mutant) from T.maritima
Structural highlights
FunctionPublication Abstract from PubMedLarge-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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