Evidence map›Paper›PMID 16524590›Full record

ArticleJournal of molecular biology2006

Structure and substrate recognition of the Escherichia coli DNA adenine methyltransferase.

John R Horton, Kirsten Liebert, Miklos Bekes, Albert Jeltsch, Xiaodong Cheng

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
3.9field-weighted citation impact, top 6% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 139 citations in OpenAlex.

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  14. Article
  15. Systematic Design of Adenosine Analogs as Inhibitors of aJournal of medicinal chemistry · 2023
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Energy Landscapes for Base-Flipping in a Model DNA Duplex.The journal of physical chemistry. B · 2022
    Article

5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

John R HortonDepartment of Biochemistry, Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA 30322, USA.
Kirsten Liebert
Miklos Bekes
Albert Jeltsch
Xiaodong Cheng
Constructor University · DEEmory University · US

Funding

THREE-DIMENSIONAL STRUCTURE OF HHAI METHYLASER01GM049245 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI CHENG, XIAODONG · 1993 to 2017
$6.6M
Histone Lysine Methylation: Structures and FunctionsR01GM068680 · NIGMS · EMORY UNIVERSITY · PI CHENG, XIAODONG · 2005 to 2012
$2.6M
NIGMS NIH HHS GM049245NIGMS NIH HHS GM068680NIGMS NIH HHS R01 GM049245NIGMS NIH HHS R01 GM068680
6 · The paper itself

Abstract

The structure of the Escherichia coli Dam DNA-(adenine-N6)-methyltransferase in complex with cognate DNA was determined at 1.89 A resolution in the presence of S-adenosyl-L-homocysteine. DNA recognition and the dynamics of base-flipping were studied by site-directed mutagenesis, DNA methylation kinetics and fluorescence stopped-flow experiments. Our data illustrate the mechanism of coupling of DNA recognition and base-flipping. Contacts to the non-target strand in the second (3') half of the GATC site are established by R124 to the fourth base-pair, and by L122 and P134 to the third base-pair. The aromatic ring of Y119 intercalates into the DNA between the second and third base-pairs, which is essential for base-flipping to occur. Compared to previous published structures of bacteriophage T4 Dam, three major new observations are made in E.coli Dam. (1) The first Gua is recognized by K9, removal of which abrogates the first base-pair recognition. (2) 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. (3) The orphaned Thy residue displays structural flexibility by adopting an extrahelical or intrahelical position where it is in contact to N120.

Indexed as

DNA, BacterialDNA MethylationEscherichia coliFluorescenceKineticsMutagenesis, Site-DirectedS-AdenosylhomocysteineSite-Specific DNA-Methyltransferase (Adenine-Specific)Substrate SpecificityDNA, BacterialS-AdenosylhomocysteineSite-Specific DNA-Methyltransferase (Adenine-Specific)

Identifiers

PMID16524590
PMCPMC2672621
OpenAlexW2078329768

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.