Structural and functional analysis show that the Escherichia coli uncharacterized protein YjcS is likely an alkylsulfatase

Protein Sci. 2014 Oct;23(10):1442-50. doi: 10.1002/pro.2528. Epub 2014 Aug 12.


Sodium dodecyl sulfate (SDS) is a widely used anionic surfactant in industry and research settings, and is known to have a detrimental effect to the environment. The pathway of SDS degradation by bacteria is initiated by an alkylsulfatase and the oxidized product, 1-dodecanoic acid, subsequently enters into the β-oxidation pathway and is used as a carbon source. In this work, we solved the crystal structure of Escherichia coli uncharacterized protein YjcS and identified that it belongs to the Type III alkylsulfatase with a signal peptide (residues 1-29) at the N terminus. YjcS hydrolyzed SDS and the double mutant D184N-H185A located in the conserved HXHXDH catalytic motif abolished this activity.

Keywords: X-ray crystallography; alkylsulfatase; hydrolase; metallo-β-lactamase; metalloenzyme.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Catalytic Domain
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Protein Structure, Tertiary
  • Sodium Dodecyl Sulfate / metabolism
  • Sulfatases / chemistry*
  • Sulfatases / genetics
  • Sulfatases / metabolism*


  • Escherichia coli Proteins
  • Sodium Dodecyl Sulfate
  • Sulfatases
  • alkylsulfatase

Associated data

  • PDB/4PDX