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Restored heptad pattern continuity does not alter the folding of a four-α-helix bundle

Nature Structural Biology volume 1, pages 706–716 (1994)Cite this article

Abstract

The sequences of α-helical coiled-coils and bundles are characterized by a specific pattern of hydrophobic and hydrophilic residues which is repeated every seven residues. Highly conserved breaks in this pattern frequently occur in segments of otherwise continuous heptad substructures. The hairpin bend of the ROP protein coincides with such a break and provides a model system for the study of the structural effects induced by heptad discontinuities. The structure of a ROP mutant which re-establishes a continuous heptad pattern, shows insignificant changes relative to the wild-type protein, as is also reflected in its conformational stability, spectroscopic properties and unfolding behaviour. Thus, formation of α-α-hairpin bends may occur both in the presence and absence of heptad breaks.

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Author notes

  1. Demetrius Tsernoglou

    Present address: Università di Roma “La Sapienza”, Dept. of Biochemistry, Piazzale A. Moro 5, I-00185, Rome, Italy

Authors and Affiliations

  1. University of Crete, Dept. of Biology and IMBB, P.O. Box 1527, GR-71110, Heraklion, Crete, Greece

    Metaxia Vlassi & Michael Kokkinidis

  2. Institut für Physikalische Chemie der Westfälischen Wilhelms-Universität, Schlossplatz 4/7, D-48149, Münster, Germany

    Christian Steif, Peter Weber & Hans-Jürgen Hinz

  3. European Molecular Biology Laboratory, Meyerhofstr. 1, D-69012, Heidelberg, Germany

    Demetrius Tsernoglou

  4. EMBL, c/o DESY, Notkestrasse 85, D-22603, Hamburg, Germany

    Keith S. Wilson

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Vlassi, M., Steif, C., Weber, P. et al. Restored heptad pattern continuity does not alter the folding of a four-α-helix bundle. Nat Struct Mol Biol 1, 706–716 (1994). https://doi.org/10.1038/nsb1094-706

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