› 3cvq

X-ray diffraction
3.01Å resolution

Structure of Peroxisomal Targeting Signal 1 (PTS1) binding domain of Trypanosoma brucei Peroxin 5 (TbPEX5)complexed to PTS1 peptide (7-SKL)

Released:
DOI: 10.2210/pdb3cvq/pdb
PDB entry 3cvq coloured by chain, front view.
PDB entry 3cvq coloured by chain, side view.
PDB entry 3cvq coloured by chain, top view.
Source organisms:
Primary publication:
Structural insights into the recognition of peroxisomal targeting signal 1 by Trypanosoma brucei peroxin 5.
Sampathkumar P, Roach C, Michels PA, Hol WG
J Mol Biol 381 867-80 (2008)
PMID: 18598704

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163467 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peroxisome targeting signal 1 receptor Chain: A
Molecule details ›
Chain: A
Length: 327 amino acids
Theoretical weight: 36.54 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q57W55 (Residues: 332-655; Coverage: 50%)
Gene names: Tb05.28F8.110, Tb927.5.1100
Sequence domains:
Structure domains: Tetratricopeptide repeat domain
PTS1 peptide 7-SKL (Ac-SNRWSKL) Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 934 Da
Source organism: Trypanosoma brucei brucei TREU927
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
1 modified residue:
Ligand SAC 1 x SAC

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P41212
Unit cell:
a: 68.794Å b: 68.794Å c: 230.232Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.275 0.273 0.321
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

11 review citations

Structural and functional discussion of the tetra-trico-peptide repeat, a protein interaction module.
Zeytuni et al. (2012)
10 more

1 mention 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)