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Literature summary extracted from

  • Nurmohamed, S.; Vaidialingam, B.; Callaghan, A.J.; Luisi, B.F.
    Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: Implications for catalytic mechanism and RNA degradosome assembly (2009), J. Mol. Biol., 389, 17-33.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.8 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.8 PNPase complexed with the recognition site from RNase E and with manganese in the presence or in the absence of modified RNA, hanging droplet vapor diffusion method, crystals for the PNPase core/RNase E micro-domain crystals are grown using 0.2 M ammonium nitrate, and 20% (w/v) PEG 3350, crystals for the PNPase core/RNase E microdomain-RNA complex are produced using 0.2 M diammonium hydrogen citrate, and 17% PEG 3350. The optimal reservoir buffer for the PNPase core/RNase E micro-domain-RNA-tungstate crystals is composed of 0.2 M di-ammonium hydrogen citrate, 17% PEG 3350, about pH 4.5, 50 mM disodium tungstate. Crystals for the PNPase core/RNase E micro-domain-Mn2+ co-crystals are prepared using 2.5 M NaCl, 9% (w/v) PEG 6000, 20 mM sodium citrate, and 20 mM manganese acetate tetrahydrate Escherichia coli
3.1.26.12 PNPase complexed with the recognition site from RNase E and with manganese in the presence or in the absence of modified RNA, hanging drop vapour diffusion method, using 0.2 M ammonium nitrate and 20% w/v PEG 3350 or 0.2 M diammonium hydrogen citrate and 17% PEG 3350 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.8 R83A the mutation has little apparent effect on activity but causes the full-length PNPase to stall on RNA oligomers shorter than eight nucleotides Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.8 Mg2+ essential cofactor for PNPase catalysis Escherichia coli
2.7.7.8 Mn2+ Mn2+ can substitute for Mg2+ as an essential co-factor for PNPase catalysis Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.8 Escherichia coli A7ZS61
-
-
3.1.26.12 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.8 ammonium sulfate precipitation, Q-Sepharose column chromatography, and Mono-Q column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.8 additional information under conditions of excess nucleoside diphosphate and low concentrations of phosphate, PNPase catalyses the reverse reaction to add 3' extensions to transcripts Escherichia coli ?
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate
-
 Escherichia coli RNAn+1 + phosphate
-
 ?
3.1.26.12 additional information a proportion of PNPase is recruited into a multi-enzyme assembly, known as the RNA degradosome, through an interaction with the scaffolding domain of the endoribonuclease RNase E Escherichia coli ?
-
 ?
3.1.26.12 RNA + H2O
-
 Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.8 trimer x-ray crystallography Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.7.8 PNPase
-
 Escherichia coli
2.7.7.8 polynucleotide phosphorylase
-
 Escherichia coli
3.1.26.12 RNase E
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.7.7.8 physiological function PNPase is a processive exoribonuclease that contributes to messenger RNA turnover and quality control of ribosomal RNA precursors Escherichia coli