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- Title
Xanthomonins I-III: A New Class of Lasso Peptides with a Seven-Residue Macrolactam Ring.
- Authors
Hegemann, Julian D.; Zimmermann, Marcel; Zhu, Shaozhou; Steuber, Holger; Harms, Klaus; Xie, Xiulan; Marahiel, Mohamed A.
- Abstract
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 structure of xanthomonin II were also determined. A total of 25 variants of xanthomonin II were generated to probe different aspects of the biosynthesis, stability, and fold maintenance. These mutational studies reveal the limits such a small ring imposes on the threading and show that every plug amino acid larger than serine is able to maintain a heat-stable lasso fold in the xanthomonin II scaffold.
- Subjects
PEPTIDES; PEPTIDE synthesis; LACTAMS; AMINO acid synthesis; HEAT stability in proteins
- Publication
Angewandte Chemie International Edition, 2014, Vol 53, Issue 8, p2230
- ISSN
1433-7851
- Publication type
Article
- DOI
10.1002/anie.201309267