Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural model for the multisubunit Type IC restriction-modification DNA methyltransferase M.EcoR124I in complex with DNA.

Nucleic acids research - 1 Jan 2006

Obarska Agnieszka, Blundell Alex, Feder Marcin, Vejsadová Stepánka, Sisáková Eva, Weiserová Marie, Bujnicki Janusz M, Firman Keith

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Proteins
Share to Conserved Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to DNA-Binding Proteins

Share to DNA Restriction-Modification Enzymes

Share to Models, Molecular

Share to Protein Subunits

Share to Sequence Alignment

Share to Site-Specific DNA-Methyltransferase (Adenine-Specific)

Source

Open in PubMed Open full text

Identifiers

PMID: 16614449
DOI: 10.1093/nar/gkl132
PMCID: PMC1435980

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural model for the multisubunit Type IC restriction-modification DNA methyltransferase M.EcoR124I in complex with DNA.PMID 16614449Read ↗

Structural insights into assembly, operation and inhibition of a type I restriction-modification system.Semantic proximity Read ↗

A residue of motif III positions the helicase domains of motor subunit HsdR in restriction-modification enzyme EcoR124I.Semantic proximity Read ↗

A novel mutant of the type I restriction-modification enzyme EcoR124I is altered at a key stage of the subunit assembly pathway.Semantic proximity Read ↗

Characterization of an EcoR124I restriction-modification enzyme produced from a deleted form of the DNA-binding subunit, which results in a novel DNA specificity.Semantic proximity Read ↗

Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I.Semantic proximity Read ↗

Identification of amino acids important for target recognition by the DNA:m5C methyltransferase M.NgoPII by alanine-scanning mutagenesis of residues at the protein-DNA interface.Semantic proximity Read ↗

Isolation of a non-classical mutant of the DNA recognition subunit of the type I restriction endonuclease R.EcoR124I.Semantic proximity Read ↗

Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme.Semantic proximity Read ↗

Expression and purification of a single-chain Type IV restriction enzyme Eco94GmrSD and determination of its substrate preference.Semantic proximity Read ↗

The DNA recognition subunit of the type IB restriction-modification enzyme EcoAI tolerates circular permutions of its polypeptide chain.Semantic proximity Read ↗

Target recognition by EcoKI: the recognition domain is robust and restriction-deficiency commonly results from the proteolytic control of enzyme activity.Semantic proximity Read ↗

A genetic dissection of the LlaJI restriction cassette reveals insights on a novel bacteriophage resistance system.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.