6cn0

X-ray diffraction
2.95Å resolution

2.95 Angstrom Crystal Structure of 16S rRNA Methylase from Proteus mirabilis

Released:
Source organism: Proteus mirabilis
Entry authors: Minasov G, Wawrzak Z, Di Leo R, Evdokimova E, Savchenko A, Satchell KJF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + guanine(1405) in 16S rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(1405) in 16S rRNA 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
16S rRNA (guanine(1405)-N(7))-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 284 amino acids
Theoretical weight: 32.42 KDa
Source organism: Proteus mirabilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q33DX5 (Residues: 1-281; Coverage: 100%)
Gene name: rmtC
Sequence domains: Ribosomal RNA methyltransferase (FmrO)

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P61
Unit cell:
a: 158.318Å b: 158.318Å c: 122.892Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.218 0.263
Expression system: Escherichia coli BL21(DE3)