Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker

Woo Hyeon Jeong, Haerim Lee, Dong Hyun Song, Jae-Hoon Eom, Sun Chang Kim, Hee-Seung Lee, Hayyoung Lee and Jie-Oh Lee ()
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Woo Hyeon Jeong: KAIST
Haerim Lee: KAIST
Dong Hyun Song: Agency for Defense Development
Jae-Hoon Eom: KAIST
Sun Chang Kim: KAIST
Hee-Seung Lee: KAIST
Hayyoung Lee: Institute of Biotechnology, Chungnam National University
Jie-Oh Lee: KAIST

Nature Communications, 2016, vol. 7, issue 1, 1-9

Abstract: Abstract Building a sophisticated protein nano-assembly requires a method for linking protein components in a predictable and stable structure. Most of the cross linkers available have flexible spacers. Because of this, the linked hybrids have significant structural flexibility and the relative structure between their two components is largely unpredictable. Here we describe a method of connecting two proteins via a ‘fusion α helix’ formed by joining two pre-existing helices into a single extended helix. Because simple ligation of two helices does not guarantee the formation of a continuous helix, we used EY-CBS, a synthetic cross linker that has been shown to react selectively with cysteines in α-helices, to stabilize the connecting helix. Formation and stabilization of the fusion helix was confirmed by determining the crystal structures of the fusion proteins with and without bound EY-CBS. Our method should be widely applicable for linking protein building blocks to generate predictable structures.

Date: 2016
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DOI: 10.1038/ncomms11031

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