› 1of9

Solution NMR

Solution structure of the pore forming toxin of entamoeba histolytica (Amoebapore A)

Released:
DOI: 10.2210/pdb1of9/pdb
PDB entry 1of9 coloured by chain, ensemble of 20 models, front view.
PDB entry 1of9 coloured by chain, ensemble of 20 models, side view.
PDB entry 1of9 coloured by chain, ensemble of 20 models, top view.
Source organism: Entamoeba histolytica
Primary publication:
Solution structure of the pore-forming protein of Entamoeba histolytica.
Hecht O, Van Nuland NA, Schleinkofer K, Dingley AJ, Bruhn H, Leippe M, Grötzinger J
J Biol Chem 279 17834-41 (2004)
PMID: 14970207

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pore-forming peptide amoebapore A Chain: A
Molecule details ›
Chain: A
Length: 77 amino acids
Theoretical weight: 8.25 KDa
Source organism: Entamoeba histolytica
UniProt:
  • Canonical: P34095 (Residues: 22-98; Coverage: 100%)
Gene name: EHI_159480
Sequence domains: Saposin-like type B, region 2
Structure domains: Saposin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry

Quick links

Citations

16 review citations

Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids.
Kolter et al. (2005)
15 more

5 mentions without citation

A short guided tour through functional and structural features of saposin-like proteins.
Bruhn H. (2005)
4 more