› 2koq

Solution NMR

NMR solution structures of 3-hydroxyoctanoyl-ACP from Streptomyces coelicolor Fatty Acid Synthase

Released:
DOI: 10.2210/pdb2koq/pdb
PDB entry 2koq coloured by chain, ensemble of 20 models, front view.
PDB entry 2koq coloured by chain, ensemble of 20 models, side view.
PDB entry 2koq coloured by chain, ensemble of 20 models, top view.
Source organism: Streptomyces coelicolor
Primary publication:
Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis.
Płoskoń E, Arthur CJ, Kanari AL, Wattana-amorn P, Williams C, Crosby J, Simpson TJ, Willis CL, Crump MP
Chem Biol 17 776-85 (2010)
PMID: 20659690

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159846 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl carrier protein Chain: A
Molecule details ›
Chain: A
Length: 81 amino acids
Theoretical weight: 8.79 KDa
Source organism: Streptomyces coelicolor
Expression system: Escherichia coli
UniProt:
  • Canonical: P72393 (Residues: 2-82; Coverage: 99%)
Gene name: acpP
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

7 review citations

The structural role of the carrier protein--active controller or passive carrier.
Crosby et al. (2012)
6 more

1 mention without citation

Structural and bioinformatic characterization of an Acinetobacter baumannii type II carrier protein.
Allen et al. (2014)