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

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

doi:10.1038/s41467-018-05441-9

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 language	English
Article number	3038
Number of pages	8
Journal	Nature Communications
Volume	9
Issue number	1
DOIs	https://doi.org/10.1038/s41467-018-05441-9
Publication status	Published - 2-Aug-2018

Keywords

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

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title = "Cysteine-mediated decyanation of vitamin B12 by the predicted membrane transporter BtuM",

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.",

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author = "Stephan Rempel and Emanuela Colucci and Gier, {Jan-Willem de} and Albert Guskov and Dirk Slotboom",

year = "2018",

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doi = "10.1038/s41467-018-05441-9",

language = "English",

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T1 - Cysteine-mediated decyanation of vitamin B12 by the predicted membrane transporter BtuM

AU - Rempel, Stephan

AU - Colucci, Emanuela

AU - Gier, Jan-Willem de

AU - Guskov, Albert

AU - Slotboom, Dirk

PY - 2018/8/2

Y1 - 2018/8/2

N2 - 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.

AB - 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.

KW - ESCHERICHIA-COLI

KW - CRYSTAL-STRUCTURE

KW - STRUCTURAL BASIS

KW - ABC TRANSPORTERS

KW - COMPLEX

KW - BINDING

KW - PROTEINS

KW - PROKARYOTES

KW - MECHANISM

KW - CLONING

U2 - 10.1038/s41467-018-05441-9

DO - 10.1038/s41467-018-05441-9

M3 - Article

SN - 2041-1723

VL - 9

JO - Nature Communications

JF - Nature Communications

IS - 1

M1 - 3038

ER -

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

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Keywords

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