Proteomics

Dataset Information

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):

ORGANISM(S): Thiobacillus Denitrificans Atcc 25259

SUBMITTER: Stephan Rempel  

LAB HEAD: Dirk Jan Slotboom

PROVIDER: PXD010024 | Pride | 2018-10-18

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
BtuM-cEPEACbl.raw Raw
BtuM-cEPEACbl.xlsx Xlsx
BtuM-cHis8-H28ACbl.raw Raw
BtuM-cHis8-H28ACbl.xlsx Xlsx
BtuM-cHis8-R153ACbl.raw Raw
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