Protein Family Models

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

Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides [1]. They are produced by bacteria of the Firmicutes phylum, and include mutacin, subtilin, and nisin. Lantibiotic peptides contain thioether bridges termed lanthionines that are thought to be generated by dehydration of serine and threonine residues followed by addition of cysteine residues [2]. This family constitutes the N-terminus of the enzyme proposed to catalyse the dehydration step [2],[3] via glutamylation of the substrate during lantibiotic biosynthesis. The enzyme dehydrates Ser/Thr residues in the precursor by glutamylation [4]. [1]. 1539969. Analysis of genes involved in biosynthesis of the lantibiotic subtilin. Klein C, Kaletta C, Schnell N, Entian KD;. Appl Environ Microbiol 1992;58:132-142. [2]. 12127987. Heterologous expression and purification of SpaB involved in subtilin biosynthesis. Xie L, Chatterjee C, Balsara R, Okeley NM, van der Donk WA;. Biochem Biophys Res Commun 2002;295:952-957. [3]. 10215865. Post-translational modification of nisin. The involvement of NisB in the dehydration process. Karakas Sen A, Narbad A, Horn N, Dodd HM, Parr AJ, Colquhoun I, Gasson MJ;. Eur J Biochem 1999;261:524-532. [4]. 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] (from Pfam)

Date:

2024-10-16

lantibiotic dehydratase is involved in the post-translational modification of lantibiotics such as epidermin and subtilin by catalyzing the dehydration of selected Ser/Thr residues of a precursor peptide

Date:

2021-02-04

This domain occurs within longer proteins that contain lantibiotic dehydratase domains (see PF04737 and PF04738), and as single-domain proteins in bacteriocin biosynthesis genomic contexts. Three named genes in this family, SioK in Streptomyces sioyaensis, TsrD in Streptomyces laurentii, and NosD in Streptomyces actuosus, all occur in regions associated with thiopeptide biosynthesis.

Date:

2020-09-29