› 2wds

X-ray diffraction
1.35Å resolution

Crystal structure of the Streptomyces coelicolor H110A AcpS mutant in complex with cofactor CoA at 1.3 A

Released:
DOI: 10.2210/pdb2wds/pdb
PDB entry 2wds coloured by chain, front view.
PDB entry 2wds coloured by chain, side view.
PDB entry 2wds coloured by chain, top view.
Source organism: Streptomyces coelicolor
Primary publication:
Analysis of Streptomyces coelicolor phosphopantetheinyl transferase, AcpS, reveals the basis for relaxed substrate specificity.
Dall'aglio P, Arthur CJ, Williams C, Vasilakis K, Maple HJ, Crosby J, Crump MP, Hadfield AT
Biochemistry 50 5704-17 (2011)
PMID: 21595442

Function and Biology Details

Reaction catalysed: 
CoA-(4'-phosphopantetheine) + an apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + an [acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131478 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Holo-[acyl-carrier-protein] synthase Chain: A
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 14.68 KDa
Source organism: Streptomyces coelicolor
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O86785 (Residues: 1-123; Coverage: 100%)
Gene names: SC6G4.22c, SCO4744, acpS
Sequence domains: 4'-phosphopantetheinyl transferase superfamily
Structure domains: 4'-phosphopantetheinyl transferase domain

Ligands and Environments

2 bound ligands:
Ligand COA 1 x COA
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P213
Unit cell:
a: 72.719Å b: 72.719Å c: 72.719Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.205
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

1 mention without citation

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life.
Beld et al. (2014)