Xanthomonins I-III: a new class of lasso peptides with a seven-residue macrolactam ring.

@article{Hegemann2014XanthomoninsIA,
  title={Xanthomonins I-III: a new class of lasso peptides with a seven-residue macrolactam ring.},
  author={Julian D. Hegemann and Marcel Zimmermann and Shaozhou Zhu and Holger Steuber and Klaus Harms and Xiulan Xie and Mohamed A. Marahiel},
  journal={Angewandte Chemie},
  year={2014},
  volume={53 8},
  pages={
          2230-4
        }
}
Lasso peptides belong to the class of ribosomally synthesized and post-translationally modified peptides. Their common distinguishing feature is an N-terminal macrolactam ring that is threaded by the C-terminal tail. This lasso fold is maintained through steric interactions. The isolation and characterization of xanthomonins I-III, the first lasso peptides featuring macrolactam rings consisting of only seven amino acids, is now presented. The crystal structure of xanthomonin I and the NMR… 
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The current state of understanding the physicochemical parameters deciding the fate of a lasso peptide at elevated temperatures is discussed, and an overview is given of the techniques developed to streamline the separation and discrimination ofLasso peptides from their branched‐cyclic topoisomers.
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The discovery of a new lasso peptide stlassin by gene activation based on a Streptomyces heterologous expression system is reported, demonstrating proof-of-concept for the combined mutational/chemical generation of lasso Peptide libraries to support drug lead development.
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The newest findings about the lasso peptides, an emerging class of ribosomally assembled and post-translationally modified peptides from bacteria that were first described in 1991 are discussed and the general methodology to elucidate these structures by NMR will be discussed and pitfalls for these approaches are highlighted.
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TLDR
A new lasso structure with a tight loop and long tail as well as narrow specificity of the maturation machinery for some essential residues associated with the protease processing site, involved in macrolactam ring formation and entrapment of the tail is revealed.
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TLDR
The structure of the most abundant lasso peptide caulosegnin I is elucidated via NMR spectroscopic analysis and a thorough mutational analysis is performed that gave insight into their biosynthesis and revealed important factors affecting the stabilization of the lasso fold in general.
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The global mutagenic approach revealed a low overall specificity of the biosynthetic machinery and important structure-stability correlations in capistruin biosynthesis.
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TLDR
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Thermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity.
TLDR
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