› 1xdn

X-ray diffraction
1.2Å resolution

High resolution crystal structure of an editosome enzyme from trypanosoma brucei: RNA editing ligase 1

Released:
DOI: 10.2210/pdb1xdn/pdb
PDB entry 1xdn coloured by chain, front view.
PDB entry 1xdn coloured by chain, side view.
PDB entry 1xdn coloured by chain, top view.
Source organism: Trypanosoma brucei
Primary publication:
High resolution crystal structure of a key editosome enzyme from Trypanosoma brucei: RNA editing ligase 1.
Deng J, Schnaufer A, Salavati R, Stuart KD, Hol WG
J Mol Biol 343 601-13 (2004)
PMID: 15465048

Function and Biology Details

Reaction catalysed: 
(1a) ATP + [RNA ligase]-L-lysine = [RNA ligase]-N(6)-(5'-adenylyl)-L-lysine + diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160988 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-editing ligase 1, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 31.54 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: P86927 (Residues: 51-324; Coverage: 58%)
Gene names: MP52, REL1, Tb09.160.2970
Sequence domains: RNA ligase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ATP 1 x ATP
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 44.911Å b: 58.579Å c: 52.984Å
α: 90° β: 100.23° γ: 90°
R-values:
R R work R free
0.129 0.128 0.148
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Complex management: RNA editing in trypanosomes.
Stuart et al. (2005)
8 more

18 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)
17 more