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Maintaining and breaking symmetry in homomeric coiled-coil assemblies

Author

Listed:
  • Guto G. Rhys

    (University of Bristol, Cantock’s Close)

  • Christopher W. Wood

    (University of Bristol, Cantock’s Close)

  • Eric J. M. Lang

    (University of Bristol, Cantock’s Close
    BrisSynBio, University of Bristol, Life Sciences Building, Tyndall Avenue)

  • Adrian J. Mulholland

    (University of Bristol, Cantock’s Close
    BrisSynBio, University of Bristol, Life Sciences Building, Tyndall Avenue
    University of Bristol, Cantock’s Close)

  • R. Leo Brady

    (School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk)

  • Andrew R. Thomson

    (University of Bristol, Cantock’s Close
    School of Chemistry, University of Glasgow)

  • Derek N. Woolfson

    (University of Bristol, Cantock’s Close
    BrisSynBio, University of Bristol, Life Sciences Building, Tyndall Avenue
    School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk)

Abstract

In coiled-coil (CC) protein structures α-helices wrap around one another to form rope-like assemblies. Most natural and designed CCs have two–four helices and cyclic (Cn) or dihedral (Dn) symmetry. Increasingly, CCs with five or more helices are being reported. A subset of these higher-order CCs is of interest as they have accessible central channels that can be functionalised; they are α-helical barrels. These extended cavities are surprising given the drive to maximise buried hydrophobic surfaces during protein folding and assembly in water. Here, we show that α-helical barrels can be maintained by the strategic placement of β-branched aliphatic residues lining the lumen. Otherwise, the structures collapse or adjust to give more-complex multi-helix assemblies without Cn or Dn symmetry. Nonetheless, the structural hallmark of CCs—namely, knobs-into-holes packing of side chains between helices—is maintained leading to classes of CCs hitherto unobserved in nature or accessed by design.

Suggested Citation

  • Guto G. Rhys & Christopher W. Wood & Eric J. M. Lang & Adrian J. Mulholland & R. Leo Brady & Andrew R. Thomson & Derek N. Woolfson, 2018. "Maintaining and breaking symmetry in homomeric coiled-coil assemblies," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06391-y
    DOI: 10.1038/s41467-018-06391-y
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    Cited by:

    1. William M. Dawson & Kathryn L. Shelley & Jordan M. Fletcher & D. Arne Scott & Lucia Lombardi & Guto G. Rhys & Tania J. LaGambina & Ulrike Obst & Antony J. Burton & Jessica A. Cross & George Davies & F, 2023. "Differential sensing with arrays of de novo designed peptide assemblies," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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