4dzr

X-ray diffraction
2.55Å resolution

The crystal structure of protein-(glutamine-N5) methyltransferase (release factor-specific) from Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446

Released:
Entry authors: Tan K, Chhor G, Bearden J, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-111832 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Release factor glutamine methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 23.8 KDa
Source organism: Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: C8WUG7 (Residues: 99-313; Coverage: 69%)
Gene names: Aaci_2779, prmC
Sequence domains: Methyltransferase small domain
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P41212
Unit cell:
a: 61.766Å b: 61.766Å c: 122.379Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.269
Expression system: Escherichia coli BL21(DE3)