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Literature summary extracted from

  • Zhang, X.; Nakashima, T.; Kakuta, Y.; Yao, M.; Tanaka, I.; Kimura, M.
    Crystal structure of an archaeal Ski2p-like protein from Pyrococcus horikoshii OT3 (2008), Protein Sci., 17, 136-145 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.4.13 overproduction of full-lenght PH1280p in Escherichia coli cells Pyrococcus horikoshii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.4.13 crystallization is carried out at 20°C by hanging-drop vapor diffusion. The crystal structure of the enzyme has been solved at a resolution of 3.5 A using single wavelength anomalous dispersion and selenomethionyl-substituted protein. Structural comparison reveals a unique arrangement of domains, a feature implicated in the specific function of the Ski2p-like RNA helicase in 3' to 5' mRNA degradation Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.13 Pyrococcus horikoshii O59025
-
-
3.6.4.13 Pyrococcus horikoshii OT-3 O59025
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.4.13
-
 Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
3.6.4.13 DNA/RNA-dependent ATPase
-
 Pyrococcus horikoshii
3.6.4.13 PH1280
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.4.13 90
-
-
 Pyrococcus horikoshii