› 1fth

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE ACYL CARRIER PROTEIN SYNTHASE (3'5'-ADP COMPLEX)

Released:
DOI: 10.2210/pdb1fth/pdb
PDB entry 1fth coloured by chain, front view.
PDB entry 1fth coloured by chain, side view.
PDB entry 1fth coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Crystal structure of Streptococcus pneumoniae acyl carrier protein synthase: an essential enzyme in bacterial fatty acid biosynthesis.
Chirgadze NY, Briggs SL, McAllister KA, Fischl AS, Zhao G
EMBO J 19 5281-7 (2000)
PMID: 11032795

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 domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141075 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Holo-[acyl-carrier-protein] synthase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 122 amino acids
Theoretical weight: 13.68 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A2W6 (Residues: 1-120; Coverage: 100%)
Gene names: SP_1699, acpS
Sequence domains: 4'-phosphopantetheinyl transferase superfamily
Structure domains: 4'-phosphopantetheinyl transferase domain

Ligands and Environments

1 bound ligand:
Ligand A3P 2 x A3P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2
Unit cell:
a: 120.188Å b: 62.273Å c: 51.673Å
α: 90° β: 98.745° γ: 90°
R-values:
R R work R free
0.238 0.238 0.275
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Biosynthesis of nonribosomal peptides1.
Finking et al. (2004)
7 more

5 mentions without citation

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