Skorupka Katarzyna, Han Seong Kyu, Nam Hyun-Jun, Kim Sanguk, Faham Salem
Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22093, USA.
Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2451-60. doi: 10.1107/S0907444913022701. Epub 2013 Nov 19.
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.
结构域融合是蛋白质设计中的一种有用工具。本文报道了异源二聚体鞭毛组装蛋白FliS和FliC融合体的结构。虽然融合蛋白维持异源二聚体结构的能力可能很明显，但基于穿线法的结构预测并不能正确融合异源二聚体。还鉴定出了与全长蛋白质同源的天然存在的异源二聚体的其他实例。这些实例表明，所设计的蛋白质是通过与蛋白质自然进化中使用的相同工具构建的，并且异源二聚体结构包含大量目前未被利用的信息，这些信息可以改善结构预测。
