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Cysteine-mediated decyanation of vitamin B12 by the predicted membrane transporter BtuM

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  • S. Rempel

    (University of Groningen)

  • E. Colucci

    (University of Groningen)

  • J. W. Gier

    (Stockholm University)

  • A. Guskov

    (University of Groningen)

  • D. J. Slotboom

    (University of Groningen
    University of Groningen)

Abstract

Uptake of vitamin B12 is essential for many prokaryotes, but in most cases the membrane proteins involved are yet to be identified. We present the biochemical characterization and high-resolution crystal structure of BtuM, a predicted bacterial vitamin B12 uptake system. BtuM binds vitamin B12 in its base-off conformation, with a cysteine residue as axial ligand of the corrin cobalt ion. Spectroscopic analysis indicates that the unusual thiolate coordination allows for decyanation of vitamin B12. Chemical modification of the substrate is a property other characterized vitamin B12-transport proteins do not exhibit.

Suggested Citation

  • S. Rempel & E. Colucci & J. W. Gier & A. Guskov & D. J. Slotboom, 2018. "Cysteine-mediated decyanation of vitamin B12 by the predicted membrane transporter BtuM," Nature Communications, Nature, vol. 9(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05441-9
    DOI: 10.1038/s41467-018-05441-9
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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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