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Structure of AMP-PNP–bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD–F

Nature Structural & Molecular Biology volume 21, pages 10971099 (2014) | Download Citation

Abstract

The reaction mechanism of BtuCD–F–catalyzed vitamin B12 transport into Escherichia coli is currently unclear. Here we present the structure of the last missing state in the form of AMP-PNP–bound BtuCD, trapped by a disulfide cross-link. Our structural and biochemical data allow a consistent mechanism to be formulated, thus rationalizing the roles of substrate, ATP and substrate-binding protein.

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Acknowledgements

This work was supported by the Swiss National Science Foundation grants SNF 31003A-116191 and SNF 31003A-146191 to K.P.L. We gratefully acknowledge the assistance of staff scientists at the PX beamline of the Swiss Light Source, Villigen, Switzerland.

Author information

Affiliations

  1. Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich, Zurich, Switzerland.

    • Vladimir M Korkhov
    • , Samantha A Mireku
    •  & Kaspar P Locher
  2. Laboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.

    • Vladimir M Korkhov
    •  & Dmitry B Veprintsev

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Contributions

V.M.K. and K.P.L. designed experiments, analyzed data and wrote the manuscript. V.M.K. and S.A.M. performed experiments, D.B.V. contributed to performing experiments, and S.A.M. contributed to data analysis and manuscript writing.

Competing interests

The authors declare no competing financial interests.

Corresponding author

Correspondence to Kaspar P Locher.

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DOI

https://doi.org/10.1038/nsmb.2918

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