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Literature summary 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

EC Number Application Comment Organism
2.1.1.72 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)

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

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.72 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
2.1.1.72 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
2.1.1.72 N120A loses its p-stacking with Gua1, shows small changes in specificity factor S1 Escherichia coli
2.1.1.72 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
2.1.1.72 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
2.1.1.72 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
2.1.1.72 Y138A loses its interaction with the O6 atom of Gua1, shows small changes in specificity factor S1 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.72 Escherichia coli P0AEE8
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

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