› 1vky

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine(34) in tRNA = L-methionine + adenine + epoxyqueuosine(34) in tRNA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine:tRNA ribosyltransferase-isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 347 amino acids
Theoretical weight: 40.18 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZ44 (Residues: 1-335; Coverage: 100%)
Gene names: TM_0574, queA
Sequence domains: Queuosine biosynthesis protein
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand UNL 2 x UNL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2, APS BEAMLINE 19-ID
Spacegroup: I222
Unit cell:
a: 119.033Å b: 122.843Å c: 131.207Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.21
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
3 more

3 mentions without citation

Natural history of S-adenosylmethionine-binding proteins.
Kozbial et al. (2005)
2 more