Abstract
Lasso peptides form a unique family of bacterial ribosomally synthesized peptides that are post-translationally modified by dedicated enzymes, which confer them a specific interlocked topology called the ‘lasso fold’ where a peptidic tail is trapped and locked into a ring. Lasso peptides typically contain around 20 amino acids, with an average size range of 15–24 amino acids (i.e. molecular weights in the range of 1500–2500 Da). The ring, comprising 7–9 amino acids (23–29 atoms), is closed by a lactam bond between the N-terminal amino group and the carboxylate side chain of a glutamate or an aspartate. The tail is trapped within the ring either by bulky side chains (steric trap**) or by one or two disulfide bonds, or by both means. This specific lasso (or lariat) topology makes lasso peptides extraordinarily stable and raises intriguing questions about the bacterial capacity to generate such an entropically disfavoured fold and how they acquired this ability in the course of evolution.
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© 2015 Yanyan Li, Séverine Zirah and Sylvie Rebuffat
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Li, Y., Zirah, S., Rebuffat, S. (2015). Introduction: A Review of Lasso Peptide Research. In: Lasso Peptides. SpringerBriefs in Microbiology. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-1010-6_1
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