Lant_dehydr_C is the C-terminal domain of a family of dehydratases that are involved in the biosynthesis of lantibiotics. While the extensive N-terminal domain, Pfam:PF04738, is involved in the serine-threonine glutamylation step of the synthetic process, this C-terminal domain, once thought to be a separate domain from the dehydratase enzymic activity, is necessary for the final glutamate-elimination step in the generation of the lantibiotic [1]. Lantibiotics are a class of peptide antibiotic that contains one or more thioether bonds. [1]. 25363770. Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB. Ortega MA, Hao Y, Zhang Q, Walker MC, van der Donk WA, Nair SK;. Nature. 2014; [Epub ahead of print]. [2]. 26877024. Structure and tRNA Specificity of MibB, a Lantibiotic Dehydratase from Actinobacteria Involved in NAI-107 Biosynthesis. Ortega MA, Hao Y, Walker MC, Donadio S, Sosio M, Nair SK, van der Donk WA;. Cell Chem Biol. 2016;23:370-380. [3]. 29158402. Structural insights into enzymatic [4+2] aza-cycloaddition in thiopeptide antibiotic biosynthesis. Cogan DP, Hudson GA, Zhang Z, Pogorelov TV, van der Donk WA, Mitchell DA, Nair SK;. Proc Natl Acad Sci U S A. 2017;114:12928-12933. [4]. 31409709. Characterization of glutamyl-tRNA-dependent dehydratases using nonreactive substrate mimics. Bothwell IR, Cogan DP, Kim T, Reinhardt CJ, van der Donk WA, Nair SK;. Proc Natl Acad Sci U S A. 2019;116:17245-17250. (from Pfam)
- Date:
- 2024-10-16