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Literature summary for 3.6.4.13 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Pyrococcus horikoshii O59025
-
-
Pyrococcus horikoshii OT-3 O59025
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus horikoshii

Synonyms

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

Temperature Optimum [°C]

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