Crystal structure of the EnvZ periplasmic domain with CHAPS

FEBS Lett. 2017 May;591(10):1419-1428. doi: 10.1002/1873-3468.12658. Epub 2017 May 9.

Abstract

Bacteria sense and respond to osmolarity through the EnvZ-OmpR two-component system. The structure of the periplasmic sensor domain of EnvZ (EnvZ-PD) is not available yet. Here, we present the crystal structure of EnvZ-PD in the presence of CHAPS detergent. The structure of EnvZ-PD shows similar folding topology to the PDC domains of PhoQ, DcuS, and CitA, but distinct orientations of helices and β-hairpin structures. The CD and NMR spectra of EnvZ-PD in the presence of cholate, a major component of bile salts, are similar to those with CHAPS. Chemical cross-linking shows that the dimerization of EnvZ-PD is significantly inhibited by the CHAPS and cholate. Together with β-galactosidase assay, these results suggest that bile salts may affect the EnvZ structure and function in Escherichia coli.

Keywords: EnvZ; X-ray crystallography; periplasmic domain.

Publication types

  • Letter

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / drug effects
  • Cholates / pharmacology*
  • Cholic Acids / pharmacology*
  • Circular Dichroism
  • Crystallography, X-Ray
  • Detergents / pharmacology*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / drug effects
  • Models, Molecular
  • Multienzyme Complexes / chemistry*
  • Multienzyme Complexes / drug effects
  • Protein Domains / drug effects
  • Protein Folding / drug effects
  • Protein Structure, Secondary / drug effects

Substances

  • Bacterial Outer Membrane Proteins
  • Cholates
  • Cholic Acids
  • Detergents
  • Escherichia coli Proteins
  • Multienzyme Complexes
  • envZ protein, E coli
  • 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate