› 1nw5

X-ray diffraction
2.05Å resolution

Structure of the beta class N6-adenine DNA methyltransferase RsrI bound to S-ADENOSYLMETHIONINE

Released:
DOI: 10.2210/pdb1nw5/pdb
PDB entry 1nw5 coloured by chain, front view.
PDB entry 1nw5 coloured by chain, side view.
PDB entry 1nw5 coloured by chain, top view.
Source organism: Cereibacter sphaeroides
Primary publication:
Structures of liganded and unliganded RsrI N6-adenine DNA methyltransferase: a distinct orientation for active cofactor binding.
Thomas CB, Scavetta RD, Gumport RI, Churchill ME
J Biol Chem 278 26094-101 (2003)
PMID: 12732637

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-147066 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type II methyltransferase M.RsrI Chain: A
Molecule details ›
Chain: A
Length: 319 amino acids
Theoretical weight: 35.7 KDa
Source organism: Cereibacter sphaeroides
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14751 (Residues: 1-319; Coverage: 100%)
Gene name: rsrIM
Sequence domains: DNA methylase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAM 1 x SAM
1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 70.36Å b: 129.06Å c: 67.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Beta class amino methyltransferases from bacteria to humans: evolution and structural consequences.
Woodcock et al. (2020)
1 more

3 mentions without citation

Structure, function and mechanism of exocyclic DNA methyltransferases.
Bheemanaik et al. (2006)
2 more