› 2fad

X-ray diffraction
1.6Å resolution

Crystal structure of E. coli heptanoyl-ACP

Released:
DOI: 10.2210/pdb2fad/pdb
PDB entry 2fad coloured by chain, front view.
PDB entry 2fad coloured by chain, side view.
PDB entry 2fad coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates.
Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR
J Mol Biol 365 135-45 (2007)
PMID: 17059829

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-141273 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl carrier protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 77 amino acids
Theoretical weight: 8.51 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6A8 (Residues: 2-78; Coverage: 99%)
Gene names: JW1080, acpP, b1094
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

3 bound ligands:
Ligand NA 1 x NA
Ligand ZN 8 x ZN
Ligand PM5 2 x PM5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 49.257Å b: 106.244Å c: 28.195Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

Membrane lipid homeostasis in bacteria.
Zhang et al. (2008)
13 more

15 mentions without citation

Fatty acid biosynthesis revisited: structure elucidation and metabolic engineering.
Beld et al. (2015)
14 more