6JDD

Crystal structure of the cypemycin decarboxylase CypD.

6JDD の概要

• エントリーDOI: 10.2210/pdb6jdd/pdb
• 分子名称: Cypemycin cysteine dehydrogenase (decarboxylating), FLAVIN-ADENINE DINUCLEOTIDE, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: decarboxylase, ripp, linaridin, biosynthetic protein
• 由来する生物種: Streptomyces sp
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21875.49

構造登録者

Zhang, Q.,Yuan, H. (登録日: 2019-02-01, 公開日: 2019-03-06, 最終更新日: 2024-03-27)

主引用文献

Mo, T.,Yuan, H.,Wang, F.,Ma, S.,Wang, J.,Li, T.,Liu, G.,Yu, S.,Tan, X.,Ding, W.,Zhang, Q.
Convergent evolution of the Cys decarboxylases involved in aminovinyl-cysteine (AviCys) biosynthesis.
FEBS Lett., 593:573-580, 2019

PubMed Abstract: 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.

PubMed: 30771247
DOI: 10.1002/1873-3468.13341

実験手法

X-RAY DIFFRACTION (2.6 Å)