ArticleNature structural biology2003
Structure of the bacteriophage T4 DNA adenine methyltransferase.
Article in Nature structural biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 48 citations in OpenAlex.
- Lineage-associated differences in adenine methylation patterns of mammalian-associatedMicrobiology spectrum · 2026Article
- A pentose, as a cytosine nucleobase modification inApplied and environmental microbiology · 2026Article
- AamA-mediated epigenetic control of genome-wide gene expression and phenotypic traits inMicrobial genomics · 2023Article
- Clostridioides difficile specific DNA adenine methyltransferase CamA squeezes and flips adenine out of DNA helix.Nature communications · 2021Article
- The cell cycle-regulated DNA adenine methyltransferase CcrM opens a bubble at its DNA recognition site.Nature communications · 2019Article
- DNA Adenine Methyltransferase (Dam) Overexpression ImpairsFrontiers in microbiology · 2017Article
- DNA base flipping analytical pipeline.Biology methods & protocols · 2017Article
- Structures of Escherichia coli DNA adenine methyltransferase (Dam) in complex with a non-GATC sequence: potential implications for methylation-independent transcriptional repression.Nucleic acids research · 2015Article
- Methyltransferases acquired by lactococcal 936-type phage provide protection against restriction endonuclease activity.BMC genomics · 2014Article
- Structural and functional insights into the molecular mechanism of rRNA m6A methyltransferase RlmJ.Nucleic acids research · 2013Article
- Time-resolved fluorescence studies of nucleotide flipping by restriction enzymes.Nucleic acids research · 2009Article
- Escherichia coli DNA adenine methyltransferase: the structural basis of processive catalysis and indirect read-out.The Journal of biological chemistry · 2009Article
- Article
- Modulation of Escherichia coli DNA methyltransferase activity by biologically derived GATC-flanking sequences.The Journal of biological chemistry · 2008Article
- Structure, function and mechanism of exocyclic DNA methyltransferases.The Biochemical journal · 2006Review
- Mutations within the catalytic motif of DNA adenine methyltransferase (Dam) of Aeromonas hydrophila cause the virulence of the Dam-overproducing strain to revert to that of the wild-type phenotype.Infection and immunity · 2006Article
- Structure and substrate recognition of the Escherichia coli DNA adenine methyltransferase.Journal of molecular biology · 2006Article
- Article
- Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions.Biological chemistry · 2004Article
- Symmetry elements in DNA structure important for recognition/methylation by DNA [amino]-methyltransferases.Nucleic acids research · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
DNA-adenine methylation at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as bacterial virulence. We report here the crystal structures of the bacteriophage T4Dam DNA adenine methyltransferase (MTase) in a binary complex with the methyl-donor product S-adenosyl-L-homocysteine (AdoHcy) and in a ternary complex with a synthetic 12-bp DNA duplex and AdoHcy. T4Dam contains two domains: a seven-stranded catalytic domain that harbors the binding site for AdoHcy and a DNA binding domain consisting of a five-helix bundle and a beta-hairpin that is conserved in the family of GATC-related MTase orthologs. Unexpectedly, the sequence-specific T4Dam bound to DNA in a nonspecific mode that contained two Dam monomers per synthetic duplex, even though the DNA contains a single GATC site. The ternary structure provides a rare snapshot of an enzyme poised for linear diffusion along the DNA.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.