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Literature summary for 6.5.1.1 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.
    View publication on PubMed
Search for more literature for 6.5.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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
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
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

Organism UniProt Comment Textmining
Pyrococcus furiosus P56709
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus furiosus

Synonyms

Synonyms Comment Organism
PfuLig
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 Pyrococcus furiosus