› 1od6

X-ray diffraction
1.5Å resolution

The Crystal Structure of Phosphopantetheine adenylyltransferase from Thermus Thermophilus in complex with 4'-phosphopantetheine

Released:
DOI: 10.2210/pdb1od6/pdb
PDB entry 1od6 coloured by chain, front view.
PDB entry 1od6 coloured by chain, side view.
PDB entry 1od6 coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus.
Takahashi H, Inagaki E, Fujimoto Y, Kuroishi C, Nodake Y, Nakamura Y, Arisaka F, Yutani K, Kuramitsu S, Yokoyama S, Yamamoto M, Miyano M, Tahirov TH
Acta Crystallogr D Biol Crystallogr 60 97-104 (2004)
PMID: 14684898

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-178038 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphopantetheine adenylyltransferase Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 17.73 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SJS9 (Residues: 1-160; Coverage: 100%)
Gene names: TTHA0929, coaD
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

2 bound ligands:
Ligand PNS 1 x PNS
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: R32
Unit cell:
a: 115.715Å b: 115.715Å c: 115.661Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.201
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

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

8 mentions without citation

Dodging the crisis of folding proteins with knots.
SuĊ‚kowska et al. (2009)
7 more