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Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase

Nature Structural Biology volume 2, pages 975–982 (1995)Cite this article

Abstract

The structure of pseudoazurin from Thiosphaera pantotropha has been determined and compared to structures of both soluble and membrane-bound periplasmic redox proteins. The results show a matching set of unipolar, but promiscuous, docking motifs based on a positive hydrophobic surface patch on the electron shuttle proteins pseudoazurin and cytochrome c550 and a negative hydrophobic patch on the surface of their known redox partners. The observed electrostatic handedness is argued to be associated with the charge-asymmetry of the membrane-bound components of the redox chain due to von Heijne's ‘positives-inside’ principle. We propose a ‘positives-in-between’ rule for electron shuttle proteins, and expect a negative hydrophobic patch to be present on both the highest and lowest redox potential species in a series of electron carriers.

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Authors and Affiliations

  1. Laboratory of Molecular Biophysics, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK

    Pamela A. Williams, Vilmos Fülöp & Janos Hajdu

  2. Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, UK

    Vilmos Fülöp, Yun-Chung Leung, Sheena E. Radford & Janos Hajdu

  3. Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK

    Christopher Chan, James W. B. Moir & Stuart J. Ferguson

  4. School of Biological Sciences, University of East Anglia, Norwich, NR4 7TJ, UK

    James W. B. Moir

  5. Department of Biochemistry and Molecular Biology, University of Melbourne, Australia

    Geoffrey Howlett

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Williams, P., Fülöp, V., Leung, YC. et al. Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase. Nat Struct Mol Biol 2, 975–982 (1995). https://doi.org/10.1038/nsb1195-975

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