Activating Compound | Comment | Organism | Structure |
---|---|---|---|
protein PhoPop5 | the enzyme is enzymatically active only when bound to proteins PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30 | Pyrococcus horikoshii | |
protein PhoRpp21 | the enzyme is enzymatically active only when bound to proteins PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30 | Pyrococcus horikoshii | |
protein PhoRpp29 | the enzyme is enzymatically active only when bound to proteins PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30 | Pyrococcus horikoshii | |
protein PhoRpp30 | the enzyme is enzymatically active only when bound to proteins PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30 | Pyrococcus horikoshii | |
protein PhoRpp38 | the enzyme is enzymatically active only when bound to proteins PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30 | Pyrococcus horikoshii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pre-tRNA + H2O | Pyrococcus horikoshii | - |
mature tRNA + 5'-terminal oligonucleotide | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O59425 and O59150 and O59543 and O59248 and P62009 | O59425: ribonuclease P protein component 1 (PhoRpp29), O59150: ribonuclease P protein component 2 (PhoPop5), O59543: ribonuclease P protein component 3 (PhoRpp30), O59248: ribonuclease P protein component 4 (RPP21), 50S ribosomal protein L7Ae (PhoRpp38). RNase P consists of a catalytic RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pre-tRNA + H2O | - |
Pyrococcus horikoshii | mature tRNA + 5'-terminal oligonucleotide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RNase P | - |
Pyrococcus horikoshii |
General Information | Comment | Organism |
---|---|---|
additional information | the secondary structure of RNase P RNA is reexamined using stringent comparative tools to arrive at phylogenetically supported model. The model structure shows an essentially flat disk with 16 tightly packed helices and a conserved face suitable for the binding of pre-tRNA. The low resolution model derived from small-angle X-ray scattering and the comparative 3-D model have similar overall shapes. The 3-D model provides a framework for a better understanding of structure-function relationships of this multifaceted primordial ribozyme | Pyrococcus horikoshii |