X-ray diffraction
1.6Å resolution

Crystal structure of Thermus thermophilus TrmFO in complex with tetrahydrofolate

Source organism: Thermus thermophilus HB8
Primary publication:
Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase.
Proc. Natl. Acad. Sci. U.S.A. 106 8180-5 (2009)
PMID: 19416846

Function and Biology Details

Reaction catalysed:
5,10-methylenetetrahydrofolate + uracil(54) in tRNA + FADH(2) = tetrahydrofolate + 5-methyluracil(54) in tRNA + FAD
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO Chain: A
Molecule details ›
Chain: A
Length: 443 amino acids
Theoretical weight: 48.92 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
  • Canonical: Q5SID2 (Residues: 1-443; Coverage: 100%)
Gene names: TTHA1442, trmFO
Sequence domains: Glucose inhibited division protein A
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments

Cofactor: Ligand FAD 1 x FAD
3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 46.809Å b: 97.023Å c: 53.794Å
α: 90° β: 101.29° γ: 90°
R R work R free
0.169 0.168 0.188
Expression system: Escherichia coli