Proteomics

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An unprecedented binding mode of vitamin B12 in the predicted transporter BtuM


ABSTRACT: BtuM binds vitamin B12 (cyano-cobalamin) in an unprecedented way. Structural and spectroscopic data indicate that the unusual thiolate coordination allows for chemical modification of the substrate, which is decyanation of the compund. We use mass-spectrometry to show the loss of the 26 Da moiety with various BtuM versions and cyano-cobalamin and dicyano-cobinamide.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Thiobacillus Denitrificans Atcc 25259

SUBMITTER: Stephan Rempel  

LAB HEAD: Dirk Jan Slotboom

PROVIDER: PXD010024 | Pride | 2018-10-18

REPOSITORIES: Pride

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Publications

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

Rempel S S   Colucci E E   de Gier J W JW   Guskov A A   Slotboom D J DJ  

Nature communications 20180802 1


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  ...[more]

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