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

Rempel, S., Colucci, E., Gier, J-W. D., Guskov, A. & Slotboom, D., 2-Aug-2018, In : Nature Communications. 9, 1, 8 p., 3038.

Research output: Contribution to journalArticleAcademicpeer-review

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.

Original languageEnglish
Article number3038
Number of pages8
JournalNature Communications
Volume9
Issue number1
Publication statusPublished - 2-Aug-2018

    Keywords

  • ESCHERICHIA-COLI, CRYSTAL-STRUCTURE, STRUCTURAL BASIS, ABC TRANSPORTERS, COMPLEX, BINDING, PROTEINS, PROKARYOTES, MECHANISM, CLONING

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