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Literature summary for 3.1.26.4 extracted from

  • Takano, K.; Okamoto, T.; Okada, J.; Tanaka, S.; Angkawidjaja, C.; Koga, Y.; Kanaya, S.
    Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag (2011), PLoS ONE, 6, e16226.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.4

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type enzyme, X-ray diffraction structure determination and analysis at 1.66-1.72 A resolution Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
C58A/C145A site-directed mutagenesis Sulfurisphaera tokodaii
additional information the Sto-RNase HI C-terminal residues, -IGCIILT, are introduced as a tag on three proteins. Each chimeric protein is more stable than its wild-type protein Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii
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-
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Synonyms

Synonyms Comment Organism
RNase HI
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 Sulfurisphaera tokodaii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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 the C-terminal of RNase HI from the hyperthermophile Sulfolobus tokodaii does not affect overall structure, and thermal stabilization is caused by local interactions of the C-terminal, suggesting that the C-terminal residues could be used as a stabilization tag. Thermodynamic measurements of the stability of variants lacking the disulfide bond, C58/145A, or the six C-terminal residues (DELTAC6) and by structural analysis of DELTAC6, overview Sulfurisphaera tokodaii