Structural highlights
Function
[MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
Publication Abstract from PubMed
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 alpha 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 alpha-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.
Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker.,Jeong WH, Lee H, Song DH, Eom JH, Kim SC, Lee HS, Lee H, Lee JO Nat Commun. 2016 Mar 16;7:11031. doi: 10.1038/ncomms11031. PMID:26980593[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jeong WH, Lee H, Song DH, Eom JH, Kim SC, Lee HS, Lee H, Lee JO. Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker. Nat Commun. 2016 Mar 16;7:11031. doi: 10.1038/ncomms11031. PMID:26980593 doi:http://dx.doi.org/10.1038/ncomms11031
