› 4chm

X-ray diffraction
2.1Å resolution

Structure of Inner Membrane Complex (IMC) Sub-compartment Protein 1 (ISP1) from Toxoplasma gondii

Released:
DOI: 10.2210/pdb4chm/pdb
PDB entry 4chm coloured by chain, front view.
PDB entry 4chm coloured by chain, side view.
PDB entry 4chm coloured by chain, top view.
Source organism: Toxoplasma gondii ME49
Primary publication:
The inner membrane complex sub-compartment proteins critical for replication of the apicomplexan parasite Toxoplasma gondii adopt a pleckstrin homology fold.
Tonkin ML, Beck JR, Bradley PJ, Boulanger MJ
J Biol Chem 289 13962-73 (2014)
PMID: 24675080

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110873 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ISP1 C-terminal domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 126 amino acids
Theoretical weight: 13.84 KDa
Source organism: Toxoplasma gondii ME49
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B9PKK4 (Residues: 58-176; Coverage: 68%)
Gene names: BN1205_073560, TGVEG_260820
Sequence domains: ISP1 C-terminal
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

1 bound ligand:
Ligand SO4 14 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-002
Spacegroup: P212121
Unit cell:
a: 58.11Å b: 81.09Å c: 120.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Post-translational modifications as key regulators of apicomplexan biology: insights from proteome-wide studies.
Yakubu et al. (2018)
7 other articles

3 mentions without citation

The apicomplexan glideosome and adhesins - Structures and function.
Boucher et al. (2015)
2 more