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 | 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 | Comment | Organism | Structure |
---|---|---|---|
cyclic di-GMP | binding at the inhibitory site mediates dimer formation and inactivation | Thermotoga maritima |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | Q9X2A8 | - |
- |
Thermotoga maritima DSM 3109 | Q9X2A8 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
TM_1788 | - |
Thermotoga maritima |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
85.5 | - |
melting temperature, wild-type | Thermotoga maritima |