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

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...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2013-12, Vol.69 (12), p.2451-2460
Main Authors: Skorupka, Katarzyna, Han, Seong Kyu, Nam, Hyun-Jun, Kim, Sanguk, Faham, Salem
Format: Article
Language:English
Subjects:
Aquifoliaceae - chemistry
Aquifoliaceae - genetics
Crystallography
Crystallography, X-Ray
Databases, Protein
Evolution, Molecular
Models, Molecular
Plant Proteins - chemistry
Plant Proteins - genetics
Protein Conformation
protein design
Protein Engineering
protein fusion
Protein Multimerization
Protein Structure, Tertiary
protein threading
Proteins
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Structural Homology, Protein
structure prediction
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Summary: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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444913022701