Metamorphic protein folding as evolutionary adaptation. Trends Biochem Sci 2023 Aug;48(8):665-672
Date
06/04/2023Pubmed ID
37270322Pubmed Central ID
PMC10526677DOI
10.1016/j.tibs.2023.05.001Scopus ID
2-s2.0-85160689793 (requires institutional sign-in at Scopus site) 1 CitationAbstract
Metamorphic proteins switch reversibly between multiple distinct, stable structures, often with different functions. It was previously hypothesized that metamorphic proteins arose as intermediates in the evolution of a new fold - rare and transient exceptions to the 'one sequence, one fold' paradigm. However, as described herein, mounting evidence suggests that metamorphic folding is an adaptive feature, preserved and optimized over evolutionary time as exemplified by the NusG family and the chemokine XCL1. Analysis of extant protein families and resurrected protein ancestors demonstrates that large regions of sequence space are compatible with metamorphic folding. As a category that enhances biological fitness, metamorphic proteins are likely to employ fold switching to perform important biological functions and may be more common than previously thought.
Author List
Dishman AF, Volkman BFAuthors
Acacia Frances Dishman MD, PhD Postdoctoral Fellow in the Biochemistry department at Medical College of WisconsinBrian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
Protein FoldingProteins
