DsbD内构象变化的证据：膜嵌入脯氨酸残基的可能作用。
Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues.
作者信息
Hiniker Annie, Vertommen Didier, Bardwell James C A, Collet Jean-Francois
机构信息
Program in Cellular and Molecular Biology, Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.
出版信息
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.
摘要
DsbD跨细胞质膜转运电子的机制尚不清楚。在此，我们提供证据表明DsbD的构象取决于其氧化状态。我们的数据还表明，围绕DsbD嵌入膜的催化半胱氨酸的四个高度保守的脯氨酸可能具有重要的功能作用，可能赋予DsbD构象灵活性。
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2
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Int J Biochem Cell Biol. 2006;38(7):1050-62. doi: 10.1016/j.biocel.2005.12.011. Epub 2006 Jan 11.
3
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6
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