› 3ett

X-ray diffraction
2.1Å resolution

Crystal structure of a bacterial arylsulfate sulfotransferase catalytic intermediate with 4-nitrophenol bound in the active site

Released:
DOI: 10.2210/pdb3ett/pdb
PDB entry 3ett coloured by chain, front view.
PDB entry 3ett coloured by chain, side view.
PDB entry 3ett coloured by chain, top view.
Source organism: Escherichia coli CFT073
Primary publication:
A structural and biochemical basis for PAPS-independent sulfuryl transfer by aryl sulfotransferase from uropathogenic Escherichia coli.
Malojcić G, Owen RL, Grimshaw JP, Brozzo MS, Dreher-Teo H, Glockshuber R
Proc Natl Acad Sci U S A 105 19217-22 (2008)
PMID: 19036922

Function and Biology Details

Reaction catalysed: 
An aryl sulfate + a phenol = a phenol + an aryl sulfate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184447 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arylsulfate sulfotransferase AssT Chains: A, B
Molecule details ›
Chains: A, B
Length: 571 amino acids
Theoretical weight: 63.93 KDa
Source organism: Escherichia coli CFT073
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8FDI4 (Residues: 28-598; Coverage: 100%)
Gene names: assT, c3785
Sequence domains:
Structure domains: Arylsulphate sulphotransferase monomer, N-terminal domain

Ligands and Environments

2 bound ligands:
Ligand NPO 2 x NPO
Ligand SO4 6 x SO4
1 modified residue:
Ligand HS8 2 x HS8

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3212
Unit cell:
a: 181.503Å b: 181.503Å c: 99.984Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.187 0.232
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Post-translational control of protein function by disulfide bond cleavage.
Cook et al. (2013)
3 more

1 mention without citation

A structural and biochemical basis for PAPS-independent sulfuryl transfer by aryl sulfotransferase from uropathogenic Escherichia coli.
Malojcić et al. (2008)