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Literature summary for 3.1.26.12 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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
RNA + H2O
-
Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
RNase E
-
Escherichia coli