Structural highlights
Function
ASTX1_ASTEC Shows weak antimicrobial activity against its phylogenetic relative Caulobacter crescentus. Does not show activity against other bacteria tested (E.coli, Vibrio sp, Burkhoderia thailandensis, and Salmonella newport).[1]
Publication Abstract from PubMed
Lasso peptides are a large family of natural products that owe their name to a unique structure formed by a side chain to backbone macrocyclization, resembling a knotted lasso. The unique structure has significant impact on their biological and physical properties, as lasso peptides are usually more stable than linear ones. Current work examines stability, structure, and biosynthesis of recently discovered lasso peptide astexin-1, a heat-sensitive lasso peptide. The obtained results revealed 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. Using the astexin-1 structure, it was possible to rationally construct a thermostable variant of this lasso peptide.
The astexin-1 lasso peptides: biosynthesis, stability, and structural studies.,Zimmermann M, Hegemann JD, Xie X, Marahiel MA Chem Biol. 2013 Apr 18;20(4):558-69. doi: 10.1016/j.chembiol.2013.03.013. PMID:23601645[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Maksimov MO, Pelczer I, Link AJ. Precursor-centric genome-mining approach for lasso peptide discovery. Proc Natl Acad Sci U S A. 2012 Sep 4. PMID:22949633 doi:http://dx.doi.org/10.1073/pnas.1208978109
- ↑ Zimmermann M, Hegemann JD, Xie X, Marahiel MA. The astexin-1 lasso peptides: biosynthesis, stability, and structural studies. Chem Biol. 2013 Apr 18;20(4):558-69. doi: 10.1016/j.chembiol.2013.03.013. PMID:23601645 doi:http://dx.doi.org/10.1016/j.chembiol.2013.03.013
