› 1sqf

X-ray diffraction
2.1Å resolution

The crystal structure of E. coli Fmu binary complex with S-Adenosylmethionine at 2.1 A resolution

Released:
DOI: 10.2210/pdb1sqf/pdb
PDB entry 1sqf coloured by chain, front view.
PDB entry 1sqf coloured by chain, side view.
PDB entry 1sqf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate.
Foster PG, Nunes CR, Greene P, Moustakas D, Stroud RM
Structure 11 1609-20 (2003)
PMID: 14656444

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + cytosine(967) in 16S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(967) in 16S rRNA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153260 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosomal RNA small subunit methyltransferase B Chain: A
Molecule details ›
Chain: A
Length: 429 amino acids
Theoretical weight: 48.41 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36929 (Residues: 1-429; Coverage: 100%)
Gene names: JW3250, b3289, fmu/fmv, rrmB, rsmB, sun, yhdB
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SAM 1 x SAM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 57.407Å b: 49.282Å c: 86.92Å
α: 90° β: 109.47° γ: 90°
R-values:
R R work R free
0.231 0.226 0.276
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

'View From A Bridge': A New Perspective on Eukaryotic rRNA Base Modification.
Sharma et al. (2015)
5 more

5 mentions without citation

5-methylcytosine in RNA: detection, enzymatic formation and biological functions.
Motorin et al. (2010)
4 more