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Acta Crystallogr. Sect. D-Biol. Crystallogr., December 2013, D69, 2451-2460 | doi:10.1107/S0907444913022701 Protein design by fusion: implications for protein structure prediction and evolution

Abstract

Katarzyna Skorupka,^a Seong Kyu Han,^b Hyun-Jun Nam,^b Sanguk Kim^b* and Salem Faham^a*

^aDepartment of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22093, USA, and ^bDivision of Molecular and Life Science, Pohang University of Science and Technology, Pohang, Republic of Korea

^*Correspondence to : Sanguk Kim, Salem 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.

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

논문정보

형식Research article
게재일2013년 12월 (BRIC 등록일 2013-11-20)
연구진국내(교신)+국외 연구진
분야 생명과학 > 유전학

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