Literature summary extracted from
Nishida, H.; Kiyonari, S.; Ishino, Y.; Morikawa, K.
The closed structure of an archaeal DNA ligase from Pyrococcus furiosus (2006), J. Mol. Biol., 360, 956-967.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
6.5.1.1 |
1.8 A resolution structure of Pyrococcus furiosus DNA ligase. The enzyme comprises the N-terminal DNA binding domain, the middle adenylation domain, and the C-terminal OB-fold domain. The architecture of each domain resembles those of human DNA ligase I, but the domain arrangements differ strikingly between the two enzymes |
Pyrococcus furiosus |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
6.5.1.1 |
K534A |
the wild-type R531A and mutant K534A enzymes exhibit almost the same DNA ligation activities both in the presence and in the absence of externally added ATP, contains AMP in the crystal |
Pyrococcus furiosus |
6.5.1.1 |
R531A |
the wild-type R531A and mutant K534A enzymes exhibit almost the same DNA ligation activities both in the presence and in the absence of externally added ATP, contains AMP in the crystal |
Pyrococcus furiosus |
6.5.1.1 |
R531A/K534A |
the mutations of both basic residues (R531A and K534A) severely affected the ligation activity, especially in the absence of ATP, does not contain AMP in the crystal |
Pyrococcus furiosus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
6.5.1.1 |
Pyrococcus furiosus |
P56709 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
6.5.1.1 |
- |
Pyrococcus furiosus |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
6.5.1.1 |
PfuLig |
- |
Pyrococcus furiosus |