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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD.
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Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD.

机译：不寻常的氧化还原活性半胱氨酸在跨膜电子转运蛋白DsbD的疏水域中的作用和位置。

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摘要

The central hydrophobic domain of the membrane protein DsbD catalyzes the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. Two cysteine residues embedded in transmembrane segments are essential for this process. Our results, based on cysteine alkylation and site-directed proteolysis, provide strong evidence that these residues are capable of forming an intramolecular disulfide bond. Also, by using a combination of two complementary genetic approaches, we show that both cysteines appear to be solvent-exposed to the cytoplasmic side of the inner membrane. These data are inconsistent with earlier topological models that place these residues on opposite sides of the membrane and permit the formulation of alternate hypotheses for the mechanism of this unusual transmembrane electron transfer.
机译：膜蛋白DsbD的中央疏水结构域催化电子从大肠埃希氏菌的细胞质转移到周质。跨膜片段中嵌入的两个半胱氨酸残基对该过程至关重要。我们基于半胱氨​​酸烷基化和定点蛋白水解的结果提供了有力的证据，这些残基能够形成分子内二硫键。同样，通过使用两种互补的遗传方法的组合，我们表明两个半胱氨酸似乎都溶剂暴露在内膜的细胞质侧。这些数据与早期的拓扑模型不一致，后者将这些残基放置在膜的相对侧，并允许为这种异常的跨膜电子转移的机理提出其他假设。

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