The application of helix fusion methods in structural biology. (February 2020)

• Record Type: Journal Article
• Authors: Kwon, Na-Young; Kim, Youngjin; Lee, Jie-Oh
• Is Part Of: Current opinion in structural biology. Volume 60(2020)
• Page Start: 110
• Page End: 116
• Publication Date: 2020-02
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2019.12.007
• Languages: English
• ISSNs: 0959-440X

Abstract

Highlights: We summarized methods connecting two pre-existing alpha helices into one continuous alpha helix. These methods can be used for crystallizing challenging target proteins including transmembrane proteins. They can be used for attaching proteins smaller than ∼50 kDa to bulkier scaffold proteins for cryo-EM analysis. Abstract : Methods generating fusion proteins with rigid and predictable structures have been developed in recent years. Among them, helix fusion methods that link two proteins by connecting their terminal alpha helices into a single and extended alpha helix can be particularly useful because designing fusion helices is conceptually and technically simple. These methods have been shown crucial in obtaining crystals that diffract x-rays to high resolution or attaching large and symmetrical backbone proteins to small target proteins for cryo-EM analysis. The structural rigidity of the fusion helix is crucial for these applications, and the reduction of structural ambiguity and flexibility at the fusion sites will further enhance the usefulness of this method.