4jak

X-ray diffraction
2Å resolution

Crystal structure of tRNA (Um34/Cm34) methyltransferase TrmL from Escherichia coli

Released:
Source organism: Escherichia coli K-12
Primary publication:
The tRNA recognition mechanism of the minimalist SPOUT methyltransferase, TrmL.
Nucleic Acids Res 41 7828-42 (2013)
PMID: 23804755

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) = S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine(34) in tRNA(Leu)
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-142836 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA (cytidine(34)-2'-O)-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 167 amino acids
Theoretical weight: 18.83 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AGJ7 (Residues: 2-157; Coverage: 99%)
Gene names: JW3581, b3606, trmL, yibK
Sequence domains: SpoU rRNA Methylase family
Structure domains: Alpha/beta knot

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P32
Unit cell:
a: 84.949Å b: 84.949Å c: 78.895Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.189 0.204
Expression system: Escherichia coli