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Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2451-60. doi: 10.1107/S0907444913022701. Epub 2013 Nov 19.

Protein design by fusion: implications for protein structure prediction and evolution.

Author information

1
Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22093, USA.

Abstract

Domain fusion is a useful tool in protein design. Here, the structure of a fusion of the heterodimeric flagella-assembly proteins FliS and FliC is reported. Although the ability of the fusion protein to maintain the structure of the heterodimer may be apparent, threading-based structural predictions do not properly fuse the heterodimer. Additional examples of naturally occurring heterodimers that are homologous to full-length proteins were identified. These examples highlight that the designed protein was engineered by the same tools as used in the natural evolution of proteins and that heterodimeric structures contain a wealth of information, currently unused, that can improve structural predictions.

KEYWORDS:

protein design; protein fusion; protein threading; structure prediction

PMID:
24311586
DOI:
10.1107/S0907444913022701
[Indexed for MEDLINE]

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