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Literature summary for 2.7.7.65 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)

Crystallization (Comment) Organism
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

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

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9X2A8
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Thermotoga maritima DSM 3109 Q9X2A8
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Synonyms

Synonyms Comment Organism
TM_1788
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Thermotoga maritima

Temperature Stability [°C]

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