EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.7.8 | expressed in Escherichia coli BL21(DE3) cells | Escherichia coli |
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 |
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 |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.8 | Escherichia coli | A7ZS61 | - |
- |
3.1.26.12 | Escherichia coli | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.7.8 | ammonium sulfate precipitation, Q-Sepharose column chromatography, and Mono-Q column chromatography | Escherichia coli |
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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.7.7.8 | trimer | x-ray crystallography | Escherichia coli |
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 |
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 |