› 1wpk

Solution NMR

Methylated Form of N-terminal Transcriptional Regulator Domain of Escherichia Coli Ada Protein

Released:
DOI: 10.2210/pdb1wpk/pdb
PDB entry 1wpk coloured by chain, ensemble of 17 models, front view.
PDB entry 1wpk coloured by chain, ensemble of 17 models, side view.
PDB entry 1wpk coloured by chain, ensemble of 17 models, top view.
Source organism: Escherichia coli
Primary publication:
The solution structure of the methylated form of the N-terminal 16-kDa domain of Escherichia coli Ada protein.
Takinowaki H, Matsuda Y, Yoshida T, Kobayashi Y, Ohkubo T
Protein Sci 15 487-97 (2006)
PMID: 16452614

Function and Biology Details

Reactions catalysed: 
DNA (containing 4-O-methylthymine) + protein L-cysteine = DNA (without 4-O-methylthymine) + protein S-methyl-L-cysteine
DNA (containing Sp-methylphosphotriester) + protein L-cysteine = DNA (without Sp-methylphosphotriester) + protein S-methyl-L-cysteine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-529477 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional transcriptional activator/DNA repair enzyme Ada Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 16.67 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P06134 (Residues: 1-146; Coverage: 41%)
Gene names: JW2201, ada, b2213
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
1 modified residue:
Ligand SMC 1 x SMC

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing, torsion angle dynamics
Expression system: Escherichia coli K-12

Quick links

Citations

4 review citations

Protein design: toward functional metalloenzymes.
Yu et al. (2014)
3 more

4 mentions without citation

Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation.
Young et al. (2012)
3 more