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Structural insights into ligand binding and gene expression control by an adenosylcobalamin riboswitch

Nature Structural & Molecular Biology volume 19, pages 11821184 (2012) | Download Citation

Abstract

Coenzyme B12 has a key role in various enzymatic reactions and controls expression of bacterial genes through riboswitches. Here we report the crystal structure of the Symbiobacterium thermophilum B12 riboswitch bound to its ligand adenosylcobalamin. The riboswitch forms a unique junctional structure with a large ligand-binding pocket tailored for specific recognition of the adenosyl moiety and flanked by structural elements that stabilize the regulatory region and enable control of gene expression.

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Acknowledgements

We thank personnel of beamlines X25 and X4C at the Brookhaven National Laboratory funded by the US Department of Energy, O. Ouerfelli (Memorial Sloan-Kettering Cancer Center) for the synthesis of iridium hexamine and E. Wasmuth for initial input into the project. A.S. was supported by funds from the New York University School of Medicine.

Author information

Affiliations

  1. Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, New York, USA.

    • Alla Peselis
    •  & Alexander Serganov

Authors

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Contributions

A.P. crystallized the AdoCbl riboswitch, A.S. determined the crystal structure. A.P. and A.S. wrote the manuscript.

Competing interests

The authors declare no competing financial interests.

Corresponding author

Correspondence to Alexander Serganov.

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DOI

https://doi.org/10.1038/nsmb.2405

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