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

Structures of liganded and unliganded RsrI N6-adenine DNA methyltransferase: a distinct orientation for active cofactor binding.

The Journal of biological chemistry - 11 Jul 2003

Thomas Chad B, Scavetta Robert D, Gumport Richard I, Churchill Mair E A

Abstract excerpt

The structures of RsrI DNA methyltransferase (M.RsrI) bound to the substrate S-adenosyl-l-methionine (AdoMet), the product S-adenosyl-l-homocysteine (AdoHcy), the inhibitor sinefungin, as well as a mutant apo-enzyme have been determined by x-ray crystallography. Two distinct binding configurations were observed for the three ligands. The substrate AdoMet adopts a bent shape that directs the activated methyl group...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine
Share to Amino Acid Motifs

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Chlorine

Share to Crystallography, X-Ray

Share to Ligands

Share to Models, Chemical

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

Source

Identifiers

PMID: 12732637
DOI: 10.1074/jbc.M303751200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structures of liganded and unliganded RsrI N6-adenine DNA methyltransferase: a distinct orientation for active cofactor binding.PMID 12732637Read ↗

Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine.Semantic proximity Read ↗

Discrimination between closely related cellular metabolites by the SAM-I riboswitch.Semantic proximity Read ↗

DNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases.Semantic proximity Read ↗

Substrate tRNA recognition mechanism of a multisite-specific tRNA methyltransferase, Aquifex aeolicus Trm1, based on the X-ray crystal structure.Semantic proximity Read ↗

Mechanism of isoprenylcysteine carboxyl methylation from the crystal structure of the integral membrane methyltransferase ICMT.Semantic proximity Read ↗

Structural and functional basis of low-affinity SAM/SAH-binding in the conserved MTase of the multi-segmented Alongshan virus distantly related to canonical unsegmented flavivirusesSemantic proximity Read ↗

Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats.Semantic proximity Read ↗

Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4).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 ↗

Insights into catalysis by a knotted TrmD tRNA methyltransferase.Semantic proximity Read ↗

Structure and dynamics of H. pylori 98-10 C5-cytosine specific DNA methyltransferase in complex with S-adenosyl-l-methionine and DNA.Semantic proximity Read ↗

Structural model of the M7G46 Methyltransferase TrmB in complex with tRNA.Semantic proximity Read ↗

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