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Literature summary extracted from

  • Xu, Y.; Amero, C.D.; Pulukkunat, D.K.; Gopalan, V.; Foster, M.P.
    Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA in (2009), J. Mol. Biol., 393, 1043-1055.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.26.5 RPP21 and RPP29. RPP29/pET-33b plasmid transformed into Escherichia coli BL21(DE3) Rosetta cells Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.26.5 A14V RPP21 mutant, wild-type RPP21 binds to RPP29 3fold tighter than the mutant Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.5 Methanocaldococcus jannaschii
-
-
-
3.1.26.5 Pyrococcus furiosus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.26.5 RPP21 and RPP29. RPP29 eluted and ultrafiltrated Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.5 pre-tRNAAsp + H2O
-
 Pyrococcus furiosus tRNAAsp + 5'-oligoribonucleotide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.26.5 ribonuclease P
-
 Pyrococcus furiosus
3.1.26.5 ribonuclease P
-
 Methanocaldococcus jannaschii
3.1.26.5 RNase P
-
 Pyrococcus furiosus
3.1.26.5 RNase P
-
 Methanocaldococcus jannaschii
3.1.26.5 Rpp21
-
 Pyrococcus furiosus
3.1.26.5 Rpp21
-
 Methanocaldococcus jannaschii
3.1.26.5 Rpp29
-
 Pyrococcus furiosus
3.1.26.5 Rpp29
-
 Methanocaldococcus jannaschii

General Information

EC Number General Information Comment Organism
3.1.26.5 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 RPP21–RPP29 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
3.1.26.5 physiological function in the presence of the RPP29–RPP21 complex, the paired regions P9, P10/11, and P12 in the S-domain are protected from V1 cleavage, while no protection by RPP29–RPP21 complex is observed in the C-domain Methanocaldococcus jannaschii