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3.1.13.4: poly(A)-specific ribonuclease

This is an abbreviated version!
For detailed information about poly(A)-specific ribonuclease, go to the full flat file.

Word Map on EC 3.1.13.4

Reaction

exonucleolytic cleavage of poly(A) to 5'-AMP =

Synonyms

2',3'-exoribonuclease, 3'-exoribonuclease, adenosine-specific exonuclease, AHG2, AtPARN, BTG1-binding factor 1, Caf1, CCR4, CCR4 deadenylase complex, CCR4-associated factor 1, Ccr4-Not complex, CCR4-NOT transcription complex subunit 7, Ccr4p/Pop2p/Notp complex, CNOT6L nuclease, cytoplasmic deadenylase, deadenylase, hPAN, HsPNLDC1, MMAR_3223, More, nuclease, polyadenylate-specific exoribo-, PAB1P-dependent poly(A)-nuclease, PAN, PAN2, PAN3, PARN, PARN-1, PARN-like domain-containing protein 1, PF2046, PNLDC1, poly(A) nuclease, poly(A) nuclease complex, poly(A) ribonuclease, poly(A)-selective ribonuclease, poly(A)-specific 3'-5' ribonuclease, poly(A)-specific 3'-exoribonuclease, poly(A)-specific mRNA exoribonuclease, poly(A)-specific ribonuclease, poly(A)-specific RNase, Pop2p deadenylase, RNase AS, RNase H

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.13 Exoribonucleases producing 5′-phosphomonoesters
                3.1.13.4 poly(A)-specific ribonuclease

Crystallization

Crystallization on EC 3.1.13.4 - poly(A)-specific ribonuclease

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the PARN-RNA-recognition motif domain (residues 445-540) with a bound 7-methylguanosine triphosphate nucleotide shows a remarkable conformational flexibility of the RNA-recognition motif domain, crystal structure is refined at a resolution of 2.1 A, protein folds into a three-stranded antiparallel beta-sheet that is flanked by one alpha-helix connecting beta-strands beta1 and beta2
free and RNA-bound forms, 20°C, hanging-drop method
in silico model for catalytic mechanism and development of a 3D pharmacophore model. Residues Arg99 and Gln109 are involved in the regulation of catalysis. The natural preference of the enzyme for poly(A) is based on favorable biophysical electrostatic and hydrophobic interactions
purified recombinant CNOT6L nuclease domain in complex with AMP and poly(A) DNA, hanging drop vapour diffusion method, 0.001 ml of protein solution, containing 15 mg/ml protein and 1 mM DTT, is mixed with 0.001 ml of reservoir solution and equilibrated over 300 ml reservoir solution, containing 0.1 M HEPES, pH 7.5, 1.1 M ammonium tartrate, and 0.2 M NDSB-201, at 16°C, X-ray diffraction structure determination and analysis at 1.94-2.44 A resolution
-
to 2.1 A resolution, one dimer per asymmetric unit
enzyme PF2046 complexed with an oligonucleotide of four thymidine nucleotides (dT4), X-ray diffraction structure determination and analysis
Pop2p crystallized by the sitting drop vapour diffusion technique, to 1.4 A resolution by X-ray crystallography, crystals belong to the space group P212121, contains a fully conserved DEDDh active site