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The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins

Nature Structural Biology volume 3, pages 267–274 (1996)Cite this article

Abstract

We use protein engineering and crystallography to simulate aspects of the early evolution of βγ-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal domain of γβ-crystallin with its four-residue C-terminal extension shows that the domain does not form a symmetric homodimer analogous to the two-domain pairing in γ-crystallins. Instead the C-terminal extension now forms heterologous interactions with other domains leading to the solvent exposure of the natural hydrophobic interface with a consequent loss in protein solubility. However, this domain truncated by just the C-terminal tyrosine forms a symmetric homodimer of domains in the crystal lattice.

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Authors and Affiliations

  1. Laboratory of Molecular Biology and ICRF Unit of Structural Molecular Biology, Department of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK

    B.V. Norledge, O.A. Bateman, C. Slingsby & H.P.C. Driessen

  2. Institut für Biophysik und Physikalische Biochemie, University of Regensburg, UniversitätsstraBe 31, D-8400, Regensburg, Germany

    E.-M. Mayr, R. Glockshuber & R. Jaenicke

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  1. B.V. Norledge
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  7. H.P.C. Driessen
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Norledge, B., Mayr, EM., Glockshuber, R. et al. The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins. Nat Struct Mol Biol 3, 267–274 (1996). https://doi.org/10.1038/nsb0396-267

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