ArticleNucleic acids research2006
Structural model for the multisubunit Type IC restriction-modification DNA methyltransferase M.EcoR124I in complex with DNA.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 21 citations in OpenAlex.
- Molecular insights into DNA recognition and methylation by non-canonical type I restriction-modification systems.Nature communications · 2022Article
- Structural insights into assembly, operation and inhibition of a type I restriction-modification system.Nature microbiology · 2020Article
- Structural basis underlying complex assembly and conformational transition of the type I R-M system.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Genome-wide survey of codons under diversifying selection in a highly recombining bacterial species, Helicobacter pylori.DNA research : an international journal for rapid publication of reports on genes and genomes · 2016Article
- Structure and operation of the DNA-translocating type I DNA restriction enzymes.Genes & development · 2012Article
- Article
- General and molecular microbiology and microbial genetics in the IM CAS.Journal of industrial microbiology & biotechnology · 2010Review
- Structural and functional analysis of the engineered type I DNA methyltransferase EcoR124IJournal of molecular biology · 2010Article
- The structure of M.EcoKI Type I DNA methyltransferase with a DNA mimic antirestriction protein.Nucleic acids research · 2009Article
- Functional analysis of MmeI from methanol utilizer Methylophilus methylotrophus, a subtype IIC restriction-modification enzyme related to type I enzymes.Applied and environmental microbiology · 2009Article
- Crystallization and preliminary X-ray diffraction analysis of the HsdR subunit of a putative type I restriction enzyme from Vibrio vulnificus YJ016.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- EcoR124I: from plasmid-encoded restriction-modification system to nanodevice.Microbiology and molecular biology reviews : MMBR · 2008Review
- HsdR subunit of the type I restriction-modification enzyme EcoR124I: biophysical characterisation and structural modelling.Journal of molecular biology · 2008Article
- DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes.The EMBO journal · 2007Article
- Shape and subunit organisation of the DNA methyltransferase M.AhdI by small-angle neutron scattering.Journal of molecular biology · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Recent publication of crystal structures for the putative DNA-binding subunits (HsdS) of the functionally uncharacterized Type I restriction-modification (R-M) enzymes MjaXIP and MgeORF438 have provided a convenient structural template for analysis of the more extensively characterized members of this interesting family of multisubunit molecular motors. Here, we present a structural model of the Type IC M.EcoR124I DNA methyltransferase (MTase), comprising the HsdS subunit, two HsdM subunits, the cofactor AdoMet and the substrate DNA molecule. The structure was obtained by docking models of individual subunits generated by fold-recognition and comparative modelling, followed by optimization of inter-subunit contacts by energy minimization. The model of M.EcoR124I has allowed identification of a number of functionally important residues that appear to be involved in DNA-binding. In addition, we have mapped onto the model the location of several new mutations of the hsdS gene of M.EcoR124I that were produced by misincorporation mutagenesis within the central conserved region of hsdS, we have mapped all previously identified DNA-binding mutants of TRD2 and produced a detailed analysis of the location of surface-modifiable lysines. The model structure, together with location of the mutant residues, provides a better background on which to study protein-protein and protein-DNA interactions in Type I R-M systems.
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.