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Literature summary for 3.4.21.B30 extracted from

  • Peat, T.S.; Frank, E.G.; McDonald, J.P.; Levine, A.S.; Woodgate, R.; Hendrickson, W.A.
    The UmuD' protein filament and its potential role in damage induced mutagenesis (1996), Structure, 4, 1401-1412.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant lacking the N-terminal extension Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli interacts with RecA-DNA filament and participates in mutagenesis ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information interacts with RecA-DNA filament and participates in mutagenesis Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dimer crystallization experiments Escherichia coli
More in addition to forming molecular dimers, the N-and C-terminal tails of UmuD' extend from a globular beta structure to associate and produce crystallized filaments. Higher oligomers are found in solution with UmuD' but not with UmuD nor with a mutant of UmuD' lacking the extended N terminus Escherichia coli