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

被引:16
|
作者
Hiniker, Annie
Vertommen, Didier
Bardwell, James C. A.
Collet, Jean-Francois
机构
[1] Univ Catholique Louvain, BCHM GRM, ICP, Unit Hormones & Metab, B-1200 Brussels, Belgium
[2] Univ Catholique Louvain, Physiol Chem Lab, Christian de Duve Inst Cellular Pathol, B-1200 Brussels, Belgium
[3] Univ Michigan, Mol & Cellular Biol Program, Dept Mol Cellular & Dev Biol, Ann Arbor, MI 48109 USA
[4] Univ Michigan, Med Scientist Training Program, Ann Arbor, MI 48109 USA
关键词
D O I
10.1128/JB.00383-06
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:7317 / 7320
页数:4
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