Open AccessLong-distance conformational changes in a protein engineered by modulated sequence duplication
Author(s) -
Martin Sagermann,
Leslie Gay,
Brian W. Matthews
Publication year - 2003
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1633549100
Subject(s) - sequence (biology) , protein engineering , protein structure , computational biology , helix (gastropod) , conformational change , scale (ratio) , protein design , mutation , mutant , computer science , biology , biophysics , genetics , physics , biochemistry , enzyme , ecology , gene , quantum mechanics , snail
There are few, if any, known instances in which a biological signal is transmitted via a large conformational change through the body of a protein. We describe here a mutant of T4 lysozyme that was engineered to permit structural change at a distance. The design uses a tandem sequence repeat that makes it possible to transmit large-scale structural changes from one end of an alpha-helix to the other over a distance of 17-25 A. The method should be of general applicability and may make it possible to introduce a mutation at one site in a protein that will induce large-scale changes in the structure at a spatially remote site.
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