Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues

J Bacteriol. 2006 Oct;188(20):7317-20. doi: 10.1128/JB.00383-06.

Abstract

The mechanism by which DsbD transports electrons across the cytoplasmic membrane is unknown. Here we provide evidence that DsbD's conformation depends on its oxidation state. Our data also suggest that four highly conserved prolines surrounding DsbD's membrane-embedded catalytic cysteines may have an important functional role, possibly conferring conformational flexibility to DsbD.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Conserved Sequence
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Molecular Sequence Data
  • Mutation
  • Oxidation-Reduction
  • Oxidoreductases / chemistry*
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism
  • Peptide Hydrolases / metabolism
  • Protein Conformation*

Substances

  • Escherichia coli Proteins
  • Oxidoreductases
  • DsbD electron transport protein, E coli
  • Peptide Hydrolases