› 1u7z

X-ray diffraction
2.3Å resolution

Phosphopantothenoylcysteine synthetase from E. coli, 4'-phosphopantothenoyl-CMP complex

Released:
DOI: 10.2210/pdb1u7z/pdb
PDB entry 1u7z coloured by chain, front view.
PDB entry 1u7z coloured by chain, side view.
PDB entry 1u7z coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis of CTP-dependent peptide bond formation in coenzyme A biosynthesis catalyzed by Escherichia coli PPC synthetase.
Stanitzek S, Augustin MA, Huber R, Kupke T, Steinbacher S
Structure 12 1977-88 (2004)
PMID: 15530362

Function and Biology Details

Reactions catalysed: 
N-((R)-4'-phosphopantothenoyl)-L-cysteine = pantotheine 4'-phosphate + CO(2)
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142188 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coenzyme A biosynthesis bifunctional protein CoaBC Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 226 amino acids
Theoretical weight: 24.83 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABQ0 (Residues: 181-406; Coverage: 56%)
Gene names: JW5642, b3639, coaBC, dfp
Sequence domains: DNA / pantothenate metabolism flavoprotein
Structure domains: CoaB-like

Ligands and Environments

1 bound ligand:
Ligand PMT 3 x PMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2221
Unit cell:
a: 43.627Å b: 142.584Å c: 244.592Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.196 0.266
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

5 mentions without citation

Relative solvent accessible surface area predicts protein conformational changes upon binding.
Marsh et al. (2011)
4 more