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Single-molecule visualization of conformational changes and substrate transport in the vitamin B12 ABC importer BtuCD-F

Author

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  • Joris M. H. Goudsmits

    (Zernike Institute for Advanced Materials, University of Groningen)

  • Dirk Jan Slotboom

    (Zernike Institute for Advanced Materials, University of Groningen
    Groningen Biomolecular Science and Biotechnology Institute, University of Groningen
    Centre for Synthetic Biology, University of Groningen)

  • Antoine M. Oijen

    (Zernike Institute for Advanced Materials, University of Groningen
    Groningen Biomolecular Science and Biotechnology Institute, University of Groningen
    Centre for Synthetic Biology, University of Groningen
    School of Chemistry, University of Wollongong)

Abstract

ATP-binding cassette (ABC) transporters form the largest class of active membrane transport proteins. Binding and hydrolysis of ATP by their highly conserved nucleotide-binding domains drive conformational changes of the complex that mediate transport of substrate across the membrane. The vitamin B12 importer BtuCD-F in Escherichia coli is an extensively studied model system. The periplasmic soluble binding protein BtuF binds the ligand; the transmembrane and ATPase domains BtuCD mediate translocation. Here we report the direct observation at the single-molecule level of ATP, vitamin B12 and BtuF-induced events in the transporter complex embedded in liposomes. Single-molecule fluorescence imaging techniques reveal that membrane-embedded BtuCD forms a stable complex with BtuF, regardless of the presence of ATP and vitamin B12. We observe that a vitamin B12 molecule remains bound to the complex for tens of seconds, during which several ATP hydrolysis cycles can take place, before it is being transported across the membrane.

Suggested Citation

  • Joris M. H. Goudsmits & Dirk Jan Slotboom & Antoine M. Oijen, 2017. "Single-molecule visualization of conformational changes and substrate transport in the vitamin B12 ABC importer BtuCD-F," Nature Communications, Nature, vol. 8(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01815-7
    DOI: 10.1038/s41467-017-01815-7
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    Cited by:

    1. Mark Nijland & Solène N. Lefebvre & Chancievan Thangaratnarajah & Dirk J. Slotboom, 2024. "Bidirectional ATP-driven transport of cobalamin by the mycobacterial ABC transporter BacA," Nature Communications, Nature, vol. 15(1), pages 1-9, December.

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