› 4bfa

X-ray diffraction
1.65Å resolution

Crystal structure of E. coli dihydrouridine synthase C (DusC)

Released:
DOI: 10.2210/pdb4bfa/pdb
PDB entry 4bfa coloured by chain, front view.
PDB entry 4bfa coloured by chain, side view.
PDB entry 4bfa coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Major reorientation of tRNA substrates defines specificity of dihydrouridine synthases.
Byrne RT, Jenkins HT, Peters DT, Whelan F, Stowell J, Aziz N, Kasatsky P, Rodnina MV, Koonin EV, Konevega AL, Antson AA
Proc Natl Acad Sci U S A 112 6033-7 (2015)
PMID: 25902496

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152604 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA-dihydrouridine(16) synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 338 amino acids
Theoretical weight: 37.7 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P33371 (Residues: 1-315; Coverage: 100%)
Gene names: JW2128, b2140, dusC, yohI
Sequence domains: Dihydrouridine synthase (Dus)
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand FMN 2 x FMN
Ligand EDO 4 x EDO
Ligand NO3 2 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 68.54Å b: 99.953Å c: 119.896Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.137 0.134 0.177
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

tRNA Modifications: Impact on Structure and Thermal Adaptation.
Lorenz et al. (2017)
6 more

6 mentions without citation

Major reorientation of tRNA substrates defines specificity of dihydrouridine synthases.
Byrne et al. (2015)
5 more