› 1t3d

X-ray diffraction
2.2Å resolution

Crystal structure of Serine Acetyltransferase from E.coli at 2.2A

Released:
DOI: 10.2210/pdb1t3d/pdb
PDB entry 1t3d coloured by chain, front view.
PDB entry 1t3d coloured by chain, side view.
PDB entry 1t3d coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure and mechanism of serine acetyltransferase from Escherichia coli.
Pye VE, Tingey AP, Robson RL, Moody PC
J Biol Chem 279 40729-36 (2004)
PMID: 15231846

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141869 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine acetyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 289 amino acids
Theoretical weight: 31.58 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9D4 (Residues: 1-273; Coverage: 100%)
Gene names: JW3582, b3607, cysE
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CYS 3 x CYS
1 modified residue:
Ligand MSE 27 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3221
Unit cell:
a: 121.98Å b: 121.98Å c: 127.52Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.151 0.177
Expression system: Escherichia coli

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Citations

7 review citations

Sulfur assimilation in photosynthetic organisms: molecular functions and regulations of transporters and assimilatory enzymes.
Takahashi et al. (2011)
6 more

15 mentions without citation

Enzymatic modifications of exopolysaccharides enhance bacterial persistence.
Whitfield et al. (2015)
14 more