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3.1.26.5: ribonuclease P

This is an abbreviated version!
For detailed information about ribonuclease P, go to the full flat file.

Word Map on EC 3.1.26.5

Reaction

endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor =

Synonyms

Aq_880, aRpp29, aRpp29 protein, AtPop1p, AtPRORP1, AtPRORP2, AtPRORP3, C5 protein, CrPRORP, hPOP1, hPOP4, hPOP7, M1 RNA, M1GS, M1GS RNA, mitochondrial RNase P protein 1, MRPP1, MRPP2, MRPP3, nuclear ribonclease P ribonucleoprotein, nuclease, ribo-, P, Pfu Pop5, PhoPRNA, POP1, Pop1p, Pop5, Pop6, Pop7, PRORP, PRORP1, PRORP2, PRORP3, Protein C5, protein-only ribonuclease P, protein-only RNase P, protein-only RNase P enzyme, proteinaceous RNase P, ribonuclease MRP, ribonuclease P, ribonuclease P ribozyme, ribosomal RNA processing ribonucleoprotein, Ribunuclease P, RNA processing protein POP1, RNA processing protein POP5, RNA processing protein POP6, RNA processing protein POP7, RNA processing protein POP8, RNase MRP, RNase P, RNase P holoenzyme, RNase P protein, RNase P ribozyme, RNase P RNA, RNase P/MRP, RNase P/MRP protein, RNaseP protein, RNaseP protein p20, RNaseP protein p30, RNaseP protein p38, RNaseP protein p40, RNases P, RNP, Rpm2p, RPP, RPP14, Rpp20, Rpp21, Rpp25, Rpp29, Rpp30, Rpp38, RPP40, RPR, RPR1, transfer RNA 5' maturation enzyme, transfer RNA processing enzyme, tRNA processing enzyme, tRNA-processing endonuclease, tRNA-processing enzyme

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.26 Endoribonucleases producing 5'-phosphomonoesters
                3.1.26.5 ribonuclease P

Crystallization

Crystallization on EC 3.1.26.5 - ribonuclease P

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of PRORP enzyme in complex with tRNA
hanging drop vapor diffusion method, crystal structure is determined at 1.7 A resolution using X-ray diffraction methods, crystals formed in space group P2(1)2(1)2(1)
crystal structure
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crystallization of the S domain of the RNA subunit, X-ray diffraction structure determination and analysis at 3.15 A resolution, structure modeling
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crystallographic structure of the S-domain of the enzyme RNA subunit
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full-length RNase P RNA of type B, to 3.3 A resolution
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the P7DELTA RNA which is comprised of the independently folding catalytic domain of the RNase P RNA is crystallized by vapour diffusion method with 50 mM Na-cacodylate at pH 6.5, 100 mM KCL, 0.7-1.0 mM spermidine tetrachloride, and 21-23% 1,6-hexanediol
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vapor diffusion method, X-ray crystal structure of ribonuclease RNA solved to 3.3 A resolution
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sitting drop vapor diffusion method at 4 °C
crystal structure analysis of PRORP enzyme in complex with tRNA
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hanging drop vapor diffusion, structure of Pfu Pop5, an archaeal RNase P protein. Crystals of Pfu Pop5 belong to the P4(1)2(1)2 space group and have five monomers in the asymmetric unit
10 mg/ml purified recombinant selenomethionine labeled protein subunit Ph1877p, vapour diffusion against 22.5% PEG 6000 and 0.1 M HEPES, pH 7.5, hanging drop method, crystals are suspended on a loop in a thin liquid film of stabilizing solution and frozen directly for X-ray diffraction structure determination and analysis at 1.8 A resolution
hanging drop vapor diffusion, structure of protein Ph1481p (subunit of RNase P) in complex with protein Ph1877p (subunit of RNase P), 2.0 A resolution
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PhoRpp21 and PhoRpp29, hanging drop vapour diffusion method. using 50 mM Tris-HCl (pH 7.5) containing 50 mM sodium chloride, 200 mM potassium nitrate, and 20% w/v PEG 3350
structure of mutant ribunuclease P protein Ph1771p, which lacks the N-terminal 31 amino acids and contains a C93S mutation is determined at 2.0 A resolution, sitting drop vapor diffusion method
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vapor diffusion against 0.2 M triammonium citrate, pH 7.0, 20% v/v polyethylene glycol 3350, 10 mM ZnCl2 and 10% v/v ethanol. Stucture of a ribonuclease P protein Ph1601p determined at 1.6 A resolution with the aid of anomalous signals from selenomethionines and zinc ion
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complex including a circularly permuted 46-nucleotide-long P3 domain of the RNA component of ribonuclease MRP and selenomethionine derivatives of the shared ribonuclease P/MRP protein components Pop6 and Pop7, using the sitting-drop vapour-diffusion method. The crystals belong to space group P4222 with unit-cell parameters a = b = 127.2, c = 76.8 A , alpha = beta = gamma = 90° and diffract to 3.25 A resolution. The terminal part of the proximal helical stem of the P3 domain is not involved in interactions with Pop6-Pop7
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3 possible RNA-binding motifs, including a putative single-stranded RNA-binding cleft formed by an alpha-helix and a four-stranded beta-sheet, derived from crystal structure and NMR study
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crystal structure analysis of RNase P enzyme in complex with tRNA, PDB ID 3Q1R
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crystal structure of the RNA component of ribonuclease P at 3.85 A resolution
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full-length RNase P RNA of type A, to 3.85 A resolution. Various coaxially stacked helices, held together by tertiary contacts, form the 3-D core that can be viewed as two single helix-thick tiers. Layer 1 encompasses both the substrate-binding regions and the putative catalytic center. Layer 2 serves as the platform for the larger layer 1 and contributes to the overall stability through tertiary interactions between the P8/P9 helical stack and the tetraloops L14 and L18. P8/P9 acts as a brace that brings together distal helices in the S (P13/P14 stack) and C domains (P18). The precise orientation of the S and C domains, facilitated by layer 2, underlies the exquisite inter-domain cooperation in substrate binding and catalysis
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