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

Stephan Rempel, Emanuela Colucci, Jan-Willem de Gier, Albert Guskov, Dirk Slotboom

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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.

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

Keywords

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

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