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› 1nw8

X-ray diffraction
2.25Å resolution

Structure of L72P mutant beta class N6-adenine DNA methyltransferase RsrI

Released:
DOI: 10.2210/pdb1nw8/pdb
Model geometry
Fit model/data
PDB entry 1nw8 coloured by chain, front view.
PDB entry 1nw8 coloured by chain, side view.
PDB entry 1nw8 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: 
a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + S-adenosyl-L-homocysteine + H(+).
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: 35.69 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

1 bound ligand:
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 71.6Å b: 131.38Å c: 67.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

1 mention without citation

Identification of an evolutionary conserved structural loop that is required for the enzymatic and biological function of tryptophan 2,3-dioxygenase.
Michels et al. (2016)