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外膜主动运输:BtuB与TonB复合物的结构

Outer membrane active transport: structure of the BtuB:TonB complex.

作者信息

Shultis David D, Purdy Michael D, Banchs Christian N, Wiener Michael C

机构信息

Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA.

出版信息

Science. 2006 Jun 2;312(5778):1396-9. doi: 10.1126/science.1127694.

Abstract

In Gram-negative bacteria, the import of essential micronutrients across the outer membrane requires a transporter, an electrochemical gradient of protons across the inner membrane, and an inner membrane protein complex (ExbB, ExbD, TonB) that couples the proton-motive force to the outer membrane transporter. The inner membrane protein TonB binds directly to a conserved region, called the Ton-box, of the transporter. We solved the structure of the cobalamin transporter BtuB in complex with the C-terminal domain of TonB. In contrast to its conformations in the absence of TonB, the Ton-box forms a beta strand that is recruited to the existing beta sheet of TonB, which is consistent with a mechanical pulling model of transport.

摘要

在革兰氏阴性菌中,必需微量营养素跨外膜的转运需要一种转运蛋白、跨内膜的质子电化学梯度以及一种将质子动力与外膜转运蛋白偶联的内膜蛋白复合物(ExbB、ExbD、TonB)。内膜蛋白TonB直接结合到转运蛋白的一个保守区域,即所谓的Ton框。我们解析了钴胺素转运蛋白BtuB与TonB C端结构域复合物的结构。与不存在TonB时的构象相比,Ton框形成一条β链,该链被招募到TonB现有的β折叠中,这与一种机械拉动转运模型一致。

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