Abstract:
:Duplication of a single β-strand that forms part of a β-sheet in photoactive yellow protein (PYP) was found to produce two approximately isoenergetic protein conformations, in which either the first or the second copy of the duplicated β-strand participates in the β-sheet. Whereas one conformation (big-loop) is more stable at equilibrium in the dark, the other conformation (long-tail) is populated after recovery from blue light irradiation. By appending a recognition motif (E-helix) to the C-terminus of the protein, we show that β-strand duplication, and the resulting possibility of β-strand slippage, can lead to a new switchable protein-protein interaction. We suggest that β-strand duplication may be a general means of introducing two-state switching activity into protein structures.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Kumar A,Nokhrin S,Woloschuk RM,Woolley GAdoi
10.1021/acs.biochem.8b00445subject
Has Abstractpub_date
2018-07-17 00:00:00pages
4093-4104issue
28eissn
0006-2960issn
1520-4995journal_volume
57pub_type
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