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Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel

Author

Listed:
  • Yi Wang

    (Ministry of Education Protein Science Laboratory,)

  • Yongjian Huang

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China)

  • Jiawei Wang

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China)

  • Chao Cheng

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China)

  • Weijiao Huang

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China)

  • Peilong Lu

    (Ministry of Education Protein Science Laboratory,)

  • Ya-Nan Xu

    (Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences)

  • Pengye Wang

    (Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences)

  • Nieng Yan

    (State Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China)

  • Yigong Shi

    (Ministry of Education Protein Science Laboratory,)

Abstract

FocA is a representative member of the formate–nitrite transporter family, which transports short-chain acids in bacteria, archaea, fungi, algae and parasites. The structure and transport mechanism of the formate–nitrite transporter family remain unknown. Here we report the crystal structure of Escherichia coli FocA at 2.25 Å resolution. FocA forms a symmetric pentamer, with each protomer consisting of six transmembrane segments. Despite a lack of sequence homology, the overall structure of the FocA protomer closely resembles that of aquaporin and strongly argues that FocA is a channel, rather than a transporter. Structural analysis identifies potentially important channel residues, defines the channel path and reveals two constriction sites. Unlike aquaporin, FocA is impermeable to water but allows the passage of formate. A structural and biochemical investigation provides mechanistic insights into the channel activity of FocA.

Suggested Citation

  • Yi Wang & Yongjian Huang & Jiawei Wang & Chao Cheng & Weijiao Huang & Peilong Lu & Ya-Nan Xu & Pengye Wang & Nieng Yan & Yigong Shi, 2009. "Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel," Nature, Nature, vol. 462(7272), pages 467-472, November.
    • Handle: RePEc:nat:nature:v:462:y:2009:i:7272:d:10.1038_nature08610
    DOI: 10.1038/nature08610
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