Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.7 extracted from

  • Hashimoto, H.; Nishioka, M.; Fujiwara, S.; Takagi, M.; Imanaka, T.; Inoue, T.; Kai, Y.
    Crystal structure of DNA polymerase from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 (2001), J. Mol. Biol., 306, 469-477.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermococcus kodakarensis

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method. The Thumb domain of DNA polymerase shows an opened conformation. The fingers subdomain possesses many basic residues at the side of the polymerase active site. The residues are considered to be accessible to the incoming dNTP by electrostatic interaction. A beta-hairpin motif (residues 242-249) extends from the exonuclease domain as seen in the editing complex of the RB69 DNA polymerase from bacteriophage RB69. Many arginine residues are located at the forked-point (the junction of the template-binding and editing clefts) of KOD DNA polymerase, suggesting that the basic environment is suitable for partitioning of the primer and template DNA duplex and for stabilizing the partially melted DNA structure in the high-temperature environments Thermococcus kodakarensis

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis P77933
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermococcus kodakarensis