Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues.
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.
Hiniker
Annie
A
Program in Cellular and Molecular Biology, Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.
Vertommen
Didier
D
Bardwell
James C A
JC
Collet
Jean-Francois
JF
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism; D011487:Protein Conformation
D029968:Escherichia coli Proteins; D010088:Oxidoreductases; C094848:DsbD electron transport protein, E coli; D010447:Peptide Hydrolases