› 2fq0

Solution NMR

Solution structure of major conformation of holo-acyl carrier protein from malaria parasite plasmodium falciparum

Released:
DOI: 10.2210/pdb2fq0/pdb
PDB entry 2fq0 coloured by chain, ensemble of 20 models, front view.
PDB entry 2fq0 coloured by chain, ensemble of 20 models, side view.
PDB entry 2fq0 coloured by chain, ensemble of 20 models, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs.
Sharma AK, Sharma SK, Surolia A, Surolia N, Sarma SP
Biochemistry 45 6904-16 (2006)
PMID: 16734426

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131248 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl carrier protein Chain: A
Molecule details ›
Chain: A
Length: 79 amino acids
Theoretical weight: 9.02 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O77077 (Residues: 59-137; Coverage: 65%)
Gene name: acpP
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

1 bound ligand:
Ligand PNS 1 x PNS
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: TORSION ANGLE DYNAMICS, SIMULATED ANNEALING
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Current understanding of fatty acid biosynthesis and the acyl carrier protein.
Chan et al. (2010)
8 more

4 mentions without citation

Plasmodium falciparum acyl carrier protein crystal structures in disulfide-linked and reduced states and their prevalence during blood stage growth.
Gallagher et al. (2010)
3 more