› 1f7l

X-ray diffraction
1.5Å resolution

HOLO-(ACYL CARRIER PROTEIN) SYNTHASE IN COMPLEX WITH COENZYME A AT 1.5A

Released:
DOI: 10.2210/pdb1f7l/pdb
PDB entry 1f7l coloured by chain, front view.
PDB entry 1f7l coloured by chain, side view.
PDB entry 1f7l coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites.
Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS
Structure 8 883-95 (2000)
PMID: 10997907

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-161229 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Holo-[acyl-carrier-protein] synthase Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.63 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P96618 (Residues: 1-121; Coverage: 100%)
Gene names: BSU04620, acpS, ydcB
Sequence domains: 4'-phosphopantetheinyl transferase superfamily
Structure domains: 4'-phosphopantetheinyl transferase domain

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand CL 1 x CL
Ligand COA 1 x COA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: R3
Unit cell:
a: 55.82Å b: 55.82Å c: 92.288Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.185 0.201
Expression system: Escherichia coli

Quick links

Citations

21 review citations

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

5 mentions without citation

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