› 4axh

X-ray diffraction
2.7Å resolution

Structure and mechanism of the first inverting alkylsulfatase specific for secondary alkylsulfatases

Released:
DOI: 10.2210/pdb4axh/pdb
PDB entry 4axh coloured by chain, front view.
PDB entry 4axh coloured by chain, side view.
PDB entry 4axh coloured by chain, top view.
Source organism: Pseudomonas sp. DSM 6611
Primary publication:
Structure and mechanism of an inverting alkylsulfatase from Pseudomonas sp. DSM6611 specific for secondary alkyl sulfates.
Knaus T, Schober M, Kepplinger B, Faccinelli M, Pitzer J, Faber K, Macheroux P, Wagner U
FEBS J 279 4374-84 (2012)
PMID: 23061549

Function and Biology Details

Reaction catalysed: 
An (R)-secondary-alkyl sulfate + H(2)O = an (S)-secondary-alcohol + sulfate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123712 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
(R)-specific secondary-alkylsulfatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 668 amino acids
Theoretical weight: 73.98 KDa
Source organism: Pseudomonas sp. DSM 6611
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: F8KAY7 (Residues: 1-660; Coverage: 100%)
Gene name: pisa1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P3121
Unit cell:
a: 141.98Å b: 141.98Å c: 119.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.221 0.266
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Inverting hydrolases and their use in enantioconvergent biotransformations.
Schober et al. (2013)
10 other articles

2 mentions without citation

Microbial alkyl- and aryl-sulfatases: mechanism, occurrence, screening and stereoselectivities.
Toesch et al. (2014)
1 more