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Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase

Author

Listed:
  • Thomas R. M. Barends

    (Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany)

  • Elisabeth Hartmann

    (Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany)

  • Julia J. Griese

    (Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany)

  • Thorsten Beitlich

    (Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany)

  • Natalia V. Kirienko

    (University of Wyoming, Laramie, Wyoming 82071, USA)

  • Dmitri A. Ryjenkov

    (University of Wyoming, Laramie, Wyoming 82071, USA)

  • Jochen Reinstein

    (Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany)

  • Robert L. Shoeman

    (Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany)

  • Mark Gomelsky

    (University of Wyoming, Laramie, Wyoming 82071, USA)

  • Ilme Schlichting

    (Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany)

Abstract

BLUF photoreceptor: light-activated scissors BLUF is a photoreceptor protein domain that uses an FAD chromophore to sense blue light. Although X-ray crystal structures of single-domain BLUF proteins have been determined, there have not been any reports of a structure of a BLUF protein that also contained a functional 'output' domain. For this reason, the mechanism(s) of light activation for this class of photoreceptors has remained enigmatic. Here, Thomas Barends and colleagues report the first biochemical, structural, and mechanistic characterization of a full-length, active photoreceptor. The protein is from the bacterium Klebsiella pneumoniae, and it contains the BLUF sensor domain and a phosphodiesterase output domain that hydrolyses cyclic dimeric GMP. The structures of this protein co-complexed with its substrate and metal ions provide a detailed understanding of how light absorbed by the BLUF domain leads to activation of the phosphodiesterase output domain.

Suggested Citation

  • Thomas R. M. Barends & Elisabeth Hartmann & Julia J. Griese & Thorsten Beitlich & Natalia V. Kirienko & Dmitri A. Ryjenkov & Jochen Reinstein & Robert L. Shoeman & Mark Gomelsky & Ilme Schlichting, 2009. "Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase," Nature, Nature, vol. 459(7249), pages 1015-1018, June.
    • Handle: RePEc:nat:nature:v:459:y:2009:i:7249:d:10.1038_nature07966
    DOI: 10.1038/nature07966
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