Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9

Biosci Rep. 2017 May 11;37(3):BSR20170001. doi: 10.1042/BSR20170001. Print 2017 Jun 30.

Abstract

A novel alkylsulfatase from bacterium Pseudomonas sp. S9 (SdsAP) was identified as a thermostable alkylsulfatases (type III), which could hydrolyze the primary alkyl sulfate such as sodium dodecyl sulfate (SDS). Thus, it has a potential application of SDS biodegradation. The crystal structure of SdsAP has been solved to a resolution of 1.76 Å and reveals that SdsAP contains the characteristic metallo-β-lactamase-like fold domain, dimerization domain, and C-terminal sterol carrier protein type 2 (SCP-2)-like fold domain. Kinetic characterization of SdsAP to SDS by isothermal titration calorimetry (ITC) and enzymatic activity assays of constructed mutants demonstrate that Y246 and G263 are important residues for its preference for the hydrolysis of 'primary alkyl' chains, confirming that SdsAP is a primary alkylsulfatase.

Keywords: Pseudomonas sp.; SCP-2-like fold domain; SDS; SdsAP; alkylsulfatase; crystal structure.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Hydrolysis
  • Kinetics
  • Pseudomonas / metabolism*
  • Sodium Dodecyl Sulfate / chemistry
  • Substrate Specificity
  • Sulfatases / chemistry*
  • Sulfates / chemistry
  • Surface-Active Agents / chemistry
  • beta-Lactamases / chemistry

Substances

  • Bacterial Proteins
  • Sulfates
  • Surface-Active Agents
  • Sodium Dodecyl Sulfate
  • Sulfatases
  • alkylsulfatase
  • beta-Lactamases