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Literature summary for 2.1.1.72 extracted from

  • Horton, J.R.; Liebert, K.; Bekes, M.; Jeltsch, A.; Cheng, X.
    Structure and substrate recognition of the Escherichia coli DNA adenine methyltransferase (2006), J. Mol. Biol., 358, 559-570.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis the first Gua is recognized by K9, removal of which abrogates the first base-pair recognition, the flipped target Ade binds to the surface of EcoDam in the absence of S-adenosyl-L-methionine, which illustrates a possible intermediate in the base-flipping pathway, the orphaned Thy residue displays structural flexibility by adopting an extrahelical or intrahelical position where it is in contact to N120 Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
His-tagged EcoDam expressed in HMS174(DE3) cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with cognate DNA at 1.89 A resolution, in the presence of S-adenosyl-L-homocysteine Escherichia coli

Protein Variants

Protein Variants Comment Organism
L122A reduces the size of an aliphatic hydrocarbon side chain, is sufficient to convert EcoDam into a bona fide maintenance MTase with pronounced preference for hemimethylated DNA Escherichia coli
additional information EcoDam K9A variant, shows slightly reduced catalytic activity and DNA binding, shows a loss of specificity at the first base-pair, unable to methylate any of the near-cognate sites, base-flipping of substrates carrying a base-pair substitution at the first position of the target site is more efficient than with wild-type Escherichia coli
N120A loses its p-stacking with Gua1, shows small changes in specificity factor S1 Escherichia coli
P134A high catalytic activity, exhibits only a small reduction in the amplitude of the fluorescence change, but no detectable changes in the kinetics of base-flipping, induces base-flipping of the substrate with altered sequence at the third base-pair Escherichia coli
P134G high catalytic activity, exhibits only a small reduction in the amplitude of the fluorescence change, but no detectable changes in the kinetics of base-flipping, induces base-flipping of the substrate with altered sequence at the third base-pair Escherichia coli
R124A overall reduction in catalytic activity but methylates the near-cognate substrates GATT and GATG faster than the canonical GATC, no base-flipping signal Escherichia coli
Y138A loses its interaction with the O6 atom of Gua1, shows small changes in specificity factor S1 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AEE8
-
-

Purification (Commentary)

Purification (Comment) Organism
by Ni2+-affinity chromatography and gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + DNA adenine
-
Escherichia coli S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
?

Synonyms

Synonyms Comment Organism
Dam
-
Escherichia coli
Dam DNA-(adenine-N6)-methyltransferase
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Escherichia coli
DNA adenine methyltransferase
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Escherichia coli
EcoDam
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Escherichia coli