› 3ne9

X-ray diffraction
2.5Å resolution

Chronobacterium ammoiniagenes apo-ACPS structure

Released:
DOI: 10.2210/pdb3ne9/pdb
PDB entry 3ne9 coloured by chain, front view.
PDB entry 3ne9 coloured by chain, side view.
PDB entry 3ne9 coloured by chain, top view.
Source organism: Corynebacterium ammoniagenes
Primary publication:
Mycobacterium tuberculosis acyl carrier protein synthase adopts two different pH-dependent structural conformations.
Gokulan K, Aggarwal A, Shipman L, Besra GS, Sacchettini JC
Acta Crystallogr D Biol Crystallogr 67 657-69 (2011)
PMID: 21697604

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128279 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Holo-[acyl-carrier-protein] synthase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 153 amino acids
Theoretical weight: 16.96 KDa
Source organism: Corynebacterium ammoniagenes
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O31302 (Residues: 1-153; Coverage: 100%)
Gene names: PPT1, acpS
Sequence domains: 4'-phosphopantetheinyl transferase superfamily
Structure domains: 4'-phosphopantetheinyl transferase domain

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P212121
Unit cell:
a: 51.399Å b: 59.002Å c: 153.561Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.268
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 citation in other articles

A phosphopantetheinyl transferase that is essential for mitochondrial fatty acid biosynthesis.
Guan et al. (2015)
7 more

3 mentions without citation

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