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Literature summary for 3.1.26.5 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
Search for more literature for 3.1.26.5

Cloned(Commentary)

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

Protein Variants

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

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
-
-
-
Pyrococcus furiosus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

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

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 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
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