› 1gn8

X-ray diffraction
1.83Å resolution

PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE IN COMPLEX WITH Mn2+ATP FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1gn8/pdb
PDB entry 1gn8 coloured by chain, front view.
PDB entry 1gn8 coloured by chain, side view.
PDB entry 1gn8 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism.
Izard T
J Mol Biol 315 487-95 (2002)
PMID: 11812124

Function and Biology Details

Reaction catalysed: 
ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141362 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphopantetheine adenylyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 17.86 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0A6I6 (Residues: 1-159; Coverage: 100%)
Gene names: JW3609, b3634, coaD, kdtB, yicA
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

3 bound ligands:
Ligand SO4 3 x SO4
Ligand ATP 2 x ATP
Ligand MN 2 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: I23
Unit cell:
a: 135.06Å b: 135.06Å c: 135.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.229 0.245

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Citations

5 review citations

Coenzyme A biosynthesis: an antimicrobial drug target.
Spry et al. (2008)
4 more

14 mentions without citation

Molecular Mechanisms for Bacterial Potassium Homeostasis.
Stautz et al. (2021)
13 more