Cloned (Comment) | Organism |
---|---|
RPP21 and RPP29. RPP29/pET-33b plasmid transformed into Escherichia coli BL21(DE3) Rosetta cells | Pyrococcus furiosus |
Protein Variants | Comment | Organism |
---|---|---|
A14V | RPP21 mutant, wild-type RPP21 binds to RPP29 3fold tighter than the mutant | Pyrococcus furiosus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanocaldococcus jannaschii | - |
- |
- |
Pyrococcus furiosus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
RPP21 and RPP29. RPP29 eluted and ultrafiltrated | Pyrococcus furiosus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pre-tRNAAsp + H2O | - |
Pyrococcus furiosus | tRNAAsp + 5'-oligoribonucleotide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ribonuclease P | - |
Pyrococcus furiosus |
ribonuclease P | - |
Methanocaldococcus jannaschii |
RNase P | - |
Pyrococcus furiosus |
RNase P | - |
Methanocaldococcus jannaschii |
Rpp21 | - |
Pyrococcus furiosus |
Rpp21 | - |
Methanocaldococcus jannaschii |
Rpp29 | - |
Pyrococcus furiosus |
Rpp29 | - |
Methanocaldococcus jannaschii |
General Information | Comment | Organism |
---|---|---|
physiological function | binding of RPP29 to RPP21 involves binding-coupled folding and stabilization of interfacial structures in RPP29. When bound to its partner, RPP21 adopts the same overall L-shaped structure observed in the free protein: a long arm containing the two N-terminal alpha-helices, a short-arm made up of the C-terminal beta-sheet comprising the zinc ribbon, and a central linker connecting the two domains. In the complex, helix alpha1 of RPP21 extends through residues 9-17, indicating that binding is associated with induced fit in RPP21 as well. The N-terminal region of RPP29 extends in an antiparallel fashion along RPP21 helix alpha1. RPP29 beta2 interacts with both helices of RPP21 in the center of the interface, and the C-terminal helix of RPP29 stabilizes the end of RPP21 helix alpha2. The RPP21RPP29 complex is localized to the specificity domain of the RNase P RNA. Sm-like core of RPP29 is essentially unchanged by RPP21 binding | Pyrococcus furiosus |
physiological function | in the presence of the RPP29RPP21 complex, the paired regions P9, P10/11, and P12 in the S-domain are protected from V1 cleavage, while no protection by RPP29RPP21 complex is observed in the C-domain | Methanocaldococcus jannaschii |