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Structure of a fucose transporter in an outward-open conformation

机译：外向构型的岩藻糖转运蛋白的结构

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摘要

The major facilitator superfamily (MFS) transporters are an ancient and widespread family of secondary active transporters. In Escherichia coli, the uptake of L-fucose, a source of carbon for microorganisms, is mediated by an MFS proton symporter, FucP. Despite intensive study of the MFS transporters, atomic structure information is only available on three proteins and the outward-open conformation has yet to be captured. Here we report the crystal structure of FucP at 3.1 A resolution, which shows that it contains an outward-open, amphipathic cavity. The similarly folded amino and carboxyl domains of FucP have contrasting surface features along the transport path, with negative electrostatic potential on the N domain and hydrophobic surface on the C domain. FucP only contains two acidic residues along the transport path, Asp 46 and Glu 135, which can undergo cycles of protonation and deprotonation. Their essential role in active transport is supported by both in vivo and in vitro experiments. Structure-based biochemical analyses provide insights into energy coupling, substrate recognition and the transport mechanism of FucP.
机译：主要促进者超家族（MFS）转运蛋白是古老且分布广泛的二级主动转运蛋白家族。在大肠杆菌中，L-岩藻糖（一种微生物碳的来源）的摄取是由MFS质子同向物FucP介导的。尽管对MFS转运蛋白进行了深入研究，但原子结构信息仅适用于三种蛋白质，并且尚未捕获向外开放的构象。在这里，我们报告了FucP在3.1 A分辨率下的晶体结构，这表明它包含一个向外开放的两亲腔。 FucP的类似折叠的氨基和羧基结构域沿传输路径具有相反的表面特征，N域具有负静电势，C域具有疏水性表面。 FucP沿运输路径仅包含两个酸性残基，Asp 46和Glu 135，它们会经历质子化和去质子化的循环。它们在主动转运中的重要作用得到体内和体外实验的支持。基于结构的生化分析可提供有关能量耦合，底物识别和FucP转运机制的见解。

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  • 来源
    《Nature》 |2010年第7316期|P.734-738|共5页
  • 作者

    Shangyu Dang; Linfeng Sun; Yongjian Huang; Feiran Lu; Yufeng Liu; Haipeng Gong; Jiawei Wang; Nieng Yan;

  • 作者单位

    State Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China;

    rnState Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China;

    rnState Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China;

    rnState Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China;

    rnState Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China;

    rnState Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China;

    rnState Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China;

    rnState Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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