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Literature summary extracted from

  • Deepthi, A.; Liew, C.W.; Liang, Z.X.; Swaminathan, K.; Lescar, J.
    Structure of a diguanylate cyclase from Thermotoga maritima: insights into activation, feedback inhibition and thermostability (2014), PLoS ONE, 9, e110912.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.65 structures of an active-like dimeric conformation with both active sites facing each other, of an inactive dimeric conformation, locked by cyclic di-GMP bound at the inhibitory site, and of a single mutant with the R158A mutation at the inhibitory site. A comparison with structurally characterized DGC homologues from mesophiles reveals the presence of a higher number of salt bridges in the hyperthermophile enzyme Thermotoga maritima

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.65 D177A mutation in salt bridge, decrease in melting temperature by 12.3 degrees Thermotoga maritima
2.7.7.65 E196A mutation in salt bridge, decrease in melting temperature by 4.2 degrees Thermotoga maritima
2.7.7.65 R158A mutation at the inhibitory site, abolishing product inhibition and unproductive dimerization Thermotoga maritima
2.7.7.65 R233A mutation in salt bridge, decrease in melting temperature by 8.6 degrees Thermotoga maritima

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.65 cyclic di-GMP binding at the inhibitory site mediates dimer formation and inactivation Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.65 Thermotoga maritima Q9X2A8
-
-
2.7.7.65 Thermotoga maritima DSM 3109 Q9X2A8
-
-

Synonyms

EC Number Synonyms Comment Organism
2.7.7.65 TM_1788
-
 Thermotoga maritima

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.7.65 85.5
-
 melting temperature, wild-type Thermotoga maritima