A Comparison of Stigmatellin Conformations, Free and Bound to the 
Photosynthetic Reaction Center and the Cytochrome bc1 Complex

Lancaster, C. Roy D.; Hunte, Carola; Kelley III, Jack; Trumpower, Bernard L.; Ditchfield, Robert

doi:10.1016/j.jmb.2007.02.013

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A Comparison of Stigmatellin Conformations, Free and Bound to the Photosynthetic Reaction Center and the Cytochrome bc₁ Complex

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Lancaster, C. Roy D.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Hunte, Carola
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Lancaster, C. R. D., Hunte, C., Kelley III, J., Trumpower, B. L., & Ditchfield, R. (2007). A Comparison of Stigmatellin Conformations, Free and Bound to the Photosynthetic Reaction Center and the Cytochrome bc₁ Complex. Journal of Molecular Biology (London), 368(1), 197-208. doi:10.1016/j.jmb.2007.02.013.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D8DB-6

Abstract

We describe in detail the conformations of the inhibitor stigmatellin in its free form and bound to the ubiquinone-reducing (Q_B) site of the reaction center and to the ubiquinol-oxidizing (Q_o) site of the cytochrome bc₁ complex. We present here the first structures of a stereochemically correct stigmatellin in complexes with a bacterial reaction center and the yeast cytochrome bc₁ complex. The conformations of the inhibitor bound to the two enzymes are not the same. We focus on the orientations of the stigmatellin side-chain relative to the chromone head group, and on the interaction of the stigmatellin side-chain with these membrane protein complexes. The different conformations of stigmatellin found illustrate the structural variability of the Q sites, which are affected by the same inhibitor. The free rotation about the χ₁ dihedral angle is an essential factor for allowing stigmatellin to bind in both the reaction center and the cytochrome bc₁ pocket.