› 3fut

X-ray diffraction
1.52Å resolution

Apo-form of T. thermophilus 16S rRNA A1518 and A1519 methyltransferase (KsgA) in space group P21212

Released:
DOI: 10.2210/pdb3fut/pdb
PDB entry 3fut coloured by chain, front view.
PDB entry 3fut coloured by chain, side view.
PDB entry 3fut coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5'-methylthioadenosine.
Demirci H, Belardinelli R, Seri E, Gregory ST, Gualerzi C, Dahlberg AE, Jogl G
J Mol Biol 388 271-82 (2009)
PMID: 19285505

Function and Biology Details

Reaction catalysed: 
4 S-adenosyl-L-methionine + adenine(1518)/adenine(1519) in 16S rRNA = 4 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(1518)/N(6)-dimethyladenine(1519) in 16S rRNA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178248 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribosomal RNA small subunit methyltransferase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 271 amino acids
Theoretical weight: 30 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SM60 (Residues: 1-271; Coverage: 100%)
Gene names: TTHA0083, ksgA, rsmA
Sequence domains: Ribosomal RNA adenine dimethylase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P21212
Unit cell:
a: 137.046Å b: 53.692Å c: 69.354Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.241
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Modification of 16S ribosomal RNA by the KsgA methyltransferase restructures the 30S subunit to optimize ribosome function.
Demirci et al. (2010)
10 more

3 mentions without citation

Crossroads between Bacterial and Mammalian Glycosyltransferases.
Brockhausen I. (2014)
2 more