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Literature summary for 2.7.7.56 extracted from

  • Choi, J.M.; Park, E.Y.; Kim, J.H.; Chang, S.K.; Cho, Y.
    Probing the functional importance of the hexameric ring structure of RNase PH (2004), J. Biol. Chem., 279, 755-764.
    View publication on PubMed
Search for more literature for 2.7.7.56

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method. The 1.9 A crystal structures of the apo and the phosphate-bound forms of RNase PH from reveal a monomeric RNase PH with an alpha/beta-fold tightly associated into a hexameric ring structure in the form of a trimer of dimers Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
R127A mutation has no influence on the structure Pseudomonas aeruginosa
R69S mutation has no influence on the structure Pseudomonas aeruginosa
R69S/R77S mutation leads to the dissociation of RNase PH hexamer into dimers without perturbing the overall monomeric structure Pseudomonas aeruginosa
R74S mutation leads to the dissociation of RNase PH hexamer into dimers without perturbing the overall monomeric structure Pseudomonas aeruginosa
R74S/R77S mutation leads to the dissociation of RNase PH hexamer into dimers without perturbing the overall monomeric structure Pseudomonas aeruginosa
R77S mutation has no influence on the structure Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
tRNAn+1 + phosphate Pseudomonas aeruginosa catalyzes the removal of nucleotides at the 3' end of the tRNA precursor, leading to the release of nucleoside diphosphate, and generates the CCA end during the maturation process tRNAn + a nucleoside diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
 recombinant enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tRNAn+1 + phosphate catalyzes the removal of nucleotides at the 3' end of the tRNA precursor, leading to the release of nucleoside diphosphate, and generates the CCA end during the maturation process Pseudomonas aeruginosa tRNAn + a nucleoside diphosphate
-
 ?

Subunits

Subunits Comment Organism
More the 1.9 A crystal structures of the apo and the phosphate-bound forms of RNase PH from reveal a monomeric RNase PH with an alpha/beta-fold tightly associated into a hexameric ring structure in the form of a trimer of dimers Pseudomonas aeruginosa

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 Tm-value for mutant enzymes R69S/R77S, R74S/R77S and R74S Pseudomonas aeruginosa
52
-
 Tm-value for wild-type enzyme and mutant enzyme R127A Pseudomonas aeruginosa