Acta Crystallographica Section D

Biological Crystallography

Volume 69, Part 12 (December 2013)

research papers

Acta Cryst. (2013). D69, 2451-2460    [ doi:10.1107/S0907444913022701 ]

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

K. Skorupka, S. K. Han, H.-J. Nam, S. Kim and S. Faham

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.

PDB reference: 4iwb

Keywords: protein design; protein fusion; protein threading; structure prediction.

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[ doi:10.1107/S0907444913022701/yt5059sup1.pdf ]
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