4NAG

Xanthomonins I III are a New Class of Lasso Peptides Featuringa Seven-Membered Macrolactam Ring

Summary for 4NAG

• Entry DOI: 10.2210/pdb4nag/pdb
• Descriptor: Xanthomonin I, HEXANE-1,6-DIOL (3 entities in total)
• Functional Keywords: biosynthesis, lasso peptides, natural products, macrocycles, steric hindrance, lariat knot, lasso fold, biosynthetic protein
• Biological source: Xanthomonas gardneri
• Total number of polymer chains: 2
• Total formula weight: 3059.34

Authors

Hegemann, J.D.,Zimmermann, M.,Zhu, S.,Steuber, H.,Harms, K.,Xie, X.,Marahiel, M.A. (deposition date: 2013-10-22, release date: 2014-04-30, Last modification date: 2024-11-27)

Primary citation

Hegemann, J.D.,Zimmermann, M.,Zhu, S.,Steuber, H.,Harms, K.,Xie, X.,Marahiel, M.A.
Xanthomonins I-III: A New Class of Lasso Peptides with a Seven-Residue Macrolactam Ring.
Angew.Chem.Int.Ed.Engl., 53:2230-2234, 2014

PubMed 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.

PubMed: 24446383
DOI: 10.1002/anie.201309267

Experimental method

X-RAY DIFFRACTION (0.81 Å)