› 4jm7

X-ray diffraction
1.82Å resolution

1.82 Angstrom resolution crystal structure of holo-(acyl-carrier-protein) synthase (acpS) from Staphylococcus aureus

Released:
DOI: 10.2210/pdb4jm7/pdb
PDB entry 4jm7 coloured by chain, front view.
PDB entry 4jm7 coloured by chain, side view.
PDB entry 4jm7 coloured by chain, top view.
Source organism: Staphylococcus aureus subsp. aureus COL
Primary publication:
Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria.
Halavaty AS, Kim Y, Minasov G, Shuvalova L, Dubrovska I, Winsor J, Zhou M, Onopriyenko O, Skarina T, Papazisi L, Kwon K, Peterson SN, Joachimiak A, Savchenko A, Anderson WF
Acta Crystallogr D Biol Crystallogr 68 1359-70 (2012)
PMID: 22993090

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-177182 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Holo-[acyl-carrier-protein] synthase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 143 amino acids
Theoretical weight: 16.37 KDa
Source organism: Staphylococcus aureus subsp. aureus COL
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5HED0 (Residues: 1-119; Coverage: 100%)
Gene names: SACOL2061, acpS
Sequence domains: 4'-phosphopantetheinyl transferase superfamily
Structure domains: 4'-phosphopantetheinyl transferase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 67.394Å b: 77.398Å c: 81.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.225
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Mining Fatty Acid Biosynthesis for New Antimicrobials.
Radka et al. (2022)
3 other articles