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Literature summary for 3.1.26.5 extracted from

  • Gobert, A.; Pinker, F.; Fuchsbauer, O.; Gutmann, B.; Boutin, R.; Roblin, P.; Sauter, C.; Giege, P.
    Structural insights into protein-only RNase P complexed with tRNA (2013), Nat. Commun., 4, 1353-1360.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.5

Protein Variants

Protein Variants Comment Organism
C344A site-directed mutagenesis, the mutant shows a 19% reduced zinc level compared to the wild-type enzyme Arabidopsis thaliana
C347A site-directed mutagenesis, the mutant shows a 29% reduced zinc level compared to the wild-type enzyme Arabidopsis thaliana
C565A site-directed mutagenesis, the mutant shows a 75% reduced zinc level compared to the wild-type enzyme Arabidopsis thaliana
C56A site-directed mutagenesis, the mutant shows no enzyme activity Arabidopsis thaliana
C56G site-directed mutagenesis, the mutant shows no enzyme activity Arabidopsis thaliana
C57A site-directed mutagenesis, the mutant shows 90% of wild-type enzyme activity Arabidopsis thaliana
C57C site-directed mutagenesis, the mutant shows 10% of wild-type enzyme activity Arabidopsis thaliana
D474A/D475A site-directed mutagenesis, the mutant shows 3,3% reduction of the zinc level compared to the wild-type enzyme Arabidopsis thaliana
G18A site-directed mutagenesis, the mutant shows 15% of wild-type enzyme activity Arabidopsis thaliana
G18C site-directed mutagenesis, the mutant shows 10% of wild-type enzyme activity Arabidopsis thaliana
G19A site-directed mutagenesis, the mutant shows 85% of wild-type enzyme activity Arabidopsis thaliana
G19C site-directed mutagenesis, the mutant shows 90% of wild-type enzyme activity Arabidopsis thaliana
H548A site-directed mutagenesis, the mutant shows a 60% reduced zinc level compared to the wild-type enzyme Arabidopsis thaliana

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ bound by conserved residues. A putative zinc-finger-like structure is split in two separate motifs. The first motif (CxxC) contains two conserved cysteines upstream of the NYN domain at positions 344 and 347 for PRORP1, whereas the second motif involves a conserved histidine and a cysteine, downstream of the NYN domain, at positions 548 and 565, respectively. The downstream conserved motif has a stronger affinity for the metal than the upstream CxxC coordination element Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q66GI4
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no ribonucleoprotein
-
 Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrates are mitochondrial tRNACys precursor variants Arabidopsis thaliana ?
-
 ?

Subunits

Subunits Comment Organism
More structure homology modelling of the enzyme's PRORP domain with bound pre-tRNACys from Escherichia coli, overview Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
PRORP1
-
 Arabidopsis thaliana
proteinaceous RNase P
-
 Arabidopsis thaliana
RNase P
-
 Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Arabidopsis thaliana

General Information

General Information Comment Organism
additional information structure-function analysis of proteinaceous RNase P, i.e. the enzyme consisting of only a protein part without catalytic RNA. The anticodon domain of transfer RNA is dispensable, whereas individual residues in D and TpsiC loops are essential for enzyme function, enzyme/transfer RNA interaction, mode of action of the proteinaceous enzyme, overview. Transfer RNA recognition by the proteinaceous PRORP enzyme is similar to that by ribonucleoprotein RNase P enzyme Arabidopsis thaliana