Lasso Peptides

Abstract

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LassoProt: server to analyze biopolymers with lassos

“…On the other hand, the function is strongly correlated with the protein structure, in particular with its entanglement pattern (e.g. in therapeutically active miniproteins ( 8 )). Thus, the LassoProt database is a useful tool for studying function-entanglement dependence.…”

“…There are many challenging questions concerning proteins with lassos, motivated also by preliminary in vivo experiments: which lasso configurations are possible, what is the role of lassos for biological function and stability of proteins, how those structures fold, etc. In addition, it is well known that therapeutic properties of some proteins can be designed by the presence of cysteine knots ( 8 ), therefore presumably complex lassos may provide new tools to steer folding and functions of proteins.…”

Identification of the Anti-Infective Aborycin Biosynthetic Gene Cluster from Deep-Sea-Derived Streptomyces sp. SCSIO ZS0098 Enables Production in a Heterologous Host

“…Predicated largely on the number of disulfide bonds in the primary structures, lasso peptides are classified as belonging in one of three possible classes [ 4 ]. Type I lasso peptides are characterized by a cyclized structure—involving linkage of the Asp9 side chain to the N-terminus of Cysl, and two disulfide bonds linking Cys1 to Cys13, and Cys7 to Cys19—to yield a tricyclic structure containing only proteinaceous amino acids [ 13 ]. Type Ⅱ lasso peptides contain no disulfide bonds and type Ⅲ lasso peptides contain only one disulfide linkage.…”

Put a Bow on It: Knotted Antibiotics Take Center Stage

“…It is not understood why class II lasso peptides are more effectively produced in an E. coli heterologous system, however those that have are also of proteobacterial origin [20,21,22,26]. The regulation of lasso peptide production strains remains poorly understood but has been reviewed to date by Li et al [27].…”