› 2b51

X-ray diffraction
2.05Å resolution

Structural Basis for UTP Specificity of RNA Editing TUTases from Trypanosoma Brucei

Released:
DOI: 10.2210/pdb2b51/pdb
PDB entry 2b51 coloured by chain, front view.
PDB entry 2b51 coloured by chain, side view.
PDB entry 2b51 coloured by chain, top view.
Source organism: Trypanosoma brucei
Primary publication:
Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei.
Deng J, Ernst NL, Turley S, Stuart KD, Hol WG
EMBO J 24 4007-17 (2005)
PMID: 16281058

Function and Biology Details

Reaction catalysed: 
UTP + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183134 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Terminal uridylyltransferase 2 Chain: A
Molecule details ›
Chain: A
Length: 468 amino acids
Theoretical weight: 54.14 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: Q86MV5 (Residues: 20-487; Coverage: 96%)
Gene names: KRET2, MP57
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MN 1 x MN
Ligand UTP 3 x UTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P41212
Unit cell:
a: 91.006Å b: 91.006Å c: 162.173Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.227
Expression system: Escherichia coli

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Citations

14 review citations

Kinetoplastids: related protozoan pathogens, different diseases.
Stuart et al. (2008)
13 more

10 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
9 more