› 8i09

X-ray diffraction
1.8Å resolution

Crystal structure of serine acetyltransferase from Salmonella typhimurium complexed with butyl gallate

Released:
DOI: 10.2210/pdb8i09/pdb
PDB entry 8i09 coloured by chain, front view.
PDB entry 8i09 coloured by chain, side view.
PDB entry 8i09 coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Alkyl gallates inhibit serine O-acetyltransferase in bacteria and enhance susceptibility of drug-resistant Gram-negative bacteria to antibiotics.
Toyomoto T, Ono K, Shiba T, Momitani K, Zhang T, Tsutsuki H, Ishikawa T, Hoso K, Hamada K, Rahman A, Wen L, Maeda Y, Yamamoto K, Matsuoka M, Hanaoka K, Niidome T, Akaike T, Sawa T
Front Microbiol 14 1276447 (2023)
PMID: 37965540

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101146 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine acetyltransferase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 280 amino acids
Theoretical weight: 30.26 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0D6I3Y9 (Residues: 2-272; Coverage: 99%)
Gene names: AAB27_17455, AU613_13940, AVC05_03655, B1P38_09830, CE70_05120, CFF59_21655, CVR97_16460, DD95_17050, DMO92_11510, DPF41_12545, DPS76_06820, DRM14_09405, DU071_11515, E0935_00610, EER35_03800, F3R12_09715, GB466_11775, GBW52_04290, SE14_03921, cysE
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand CYS 12 x CYS
Ligand NF0 12 x NF0
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 177.363Å b: 102.649Å c: 158.715Å
α: 90° β: 111.85° γ: 90°
R-values:
R R work R free
0.205 0.204 0.241
Expression system: Escherichia coli

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