Convergent evolution of the Cys decarboxylases involved in aminovinyl-cysteine (AviCys) biosynthesis

FEBS Letters

article

Tianlu Mo¹  Hong Yuan¹  Fangting Wang¹  Suze Ma¹  Jinxiu Wang¹  Ting Li¹  Guangfeng Liu³  Shaoning Yu¹  Xiangshi Tan¹  Wei Ding¹  Qi Zhang¹ 

[1] Department of Chemistry, Fudan University;State Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University;National Center for Protein Science

关键词: decarboxylase;    enzyme evolution;    HFCD;    natural product biosynthesis;    RiPP;   

DOI  :  10.1002/1873-3468.13341

来源: John Wiley & Sons Ltd.

【 摘 要 】

S-[(Z)-2-aminovinyl]-D-cysteine (AviCys) is a unique motif found in several classes of ribosomally synthesized and post-translationally modified peptides (RiPPs). Biosynthesis of AviCys requires flavin-dependent Cys decarboxylases, which are highly divergent among different RiPP classes. In this study, we solved the crystal structure of the cypemycin decarboxylase CypD. We show that CypD is structurally highly similar to lanthipeptide decarboxylases despite the absence of sequence similarities between them. We further show that Cys decarboxylases from four RiPP classes have evolved independently and form two major clusters. These results reveal the convergent evolution of AviCys biosynthesis and suggest that all the flavin-dependent Cys decarboxylases likely have a similar Rossmann fold despite their sequence divergences.

【 授权许可】

Unknown