Literature summary 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.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.7.56 |
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
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.7.56 |
R127A |
mutation has no influence on the structure |
Pseudomonas aeruginosa |
2.7.7.56 |
R69S |
mutation has no influence on the structure |
Pseudomonas aeruginosa |
2.7.7.56 |
R69S/R77S |
mutation leads to the dissociation of RNase PH hexamer into dimers without perturbing the overall monomeric structure |
Pseudomonas aeruginosa |
2.7.7.56 |
R74S |
mutation leads to the dissociation of RNase PH hexamer into dimers without perturbing the overall monomeric structure |
Pseudomonas aeruginosa |
2.7.7.56 |
R74S/R77S |
mutation leads to the dissociation of RNase PH hexamer into dimers without perturbing the overall monomeric structure |
Pseudomonas aeruginosa |
2.7.7.56 |
R77S |
mutation has no influence on the structure |
Pseudomonas aeruginosa |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.7.7.56 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.7.56 |
Pseudomonas aeruginosa |
- |
recombinant enzyme |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.7.56 |
recombinant enzyme |
Pseudomonas aeruginosa |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.7.56 |
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
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.7.56 |
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]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
2.7.7.56 |
45 |
- |
Tm-value for mutant enzymes R69S/R77S, R74S/R77S and R74S |
Pseudomonas aeruginosa |
2.7.7.56 |
52 |
- |
Tm-value for wild-type enzyme and mutant enzyme R127A |
Pseudomonas aeruginosa |