Chaperoning the major facilitator superfamily at single-molecule level.

Structure

Department of Chemistry, Ulsan National Institute of Science and Technology, Ulsan 44919, Republic of Korea; Center for Wave Energy Materials, Ulsan National Institute of Science and Technology, Ulsan 44919, Republic of Korea. Electronic address:

Published: November 2023

In this issue of Structure, Blaimschein et al. elucidate the chaperoning function of the insertase YidC during the insertion and folding of the melibiose permease MelB. Their single-molecule forced unfolding approach reveals that YidC significantly reduces the misfolding and enhances the folding of helices near the interface of two folding cores.

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http://dx.doi.org/10.1016/j.str.2023.10.003DOI Listing

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