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Literature summary extracted from

  • Zhou, Z.; Feng, H.; Ghirlando, R.; Bai, Y.
    The high-resolution NMR structure of the early folding intermediate of the Thermus thermophilus ribonuclease H (2008), J. Mol. Biol., 384, 531-539.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.1.26.4 additional information populating the folded region of the intermediate mimic by protein engineering Thermus thermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.26.4 12800
-
 intermediate mimic, ultracentrifugation experiments Thermus thermophilus
3.1.26.4 13000
-
 intermediate mimic, gel filtration Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.4 Thermus thermophilus P29253
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.26.4 using Ni-NTA agarose and reverse-phase HPLC Thermus thermophilus

Subunits

EC Number Subunits Comment Organism
3.1.26.4 monomer enzyme is composed of five alpha-helices (A to E) and five beta-strands (I to V). The intermediate mimic is a monomer Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
3.1.26.4 ribonuclease H
-
 Thermus thermophilus
3.1.26.4 RNase H
-
 Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.26.4 75
-
 melting temperature curve of the intermediate mimic shown. The heat denaturation experiment shows that this intermediate mimic unfolds cooperatively as temperature increases, with a melting temperature (Tm) of about 75°C Thermus thermophilus