Moenomycin‐type antibiotics are phosphoglycolipids that are notable for their unique modes of action and have proven to be useful in animal nutrition. The gene clusters tchm from Actinoplanes teichomyceticus and moe from Streptomyces are among a limited number of known moenomycin‐biosynthetic pathways. Most genes in tchm have counterparts in the moe cluster, except for tchmy and tchmz, the functions of which remain unknown. Sequence analysis indicates that TchmY belongs to the isoprenoid enzyme C2‐like superfamily and may serve as a prenylcyclase. The enzyme was proposed to be involved in terminal cyclization of the moenocinyl chain in teichomycin, leading to the diumycinol chain of moenomycin isomers. Here, recombinant TchmY protein was expressed in Escherichia coli and its crystal structure was solved by SIRAS. Structural analysis and comparison with other prenylcyclases were performed. The overall fold of TchmY consists of an (α/α)₆‐barrel, and a potential substrate‐binding pocket is found in the central chamber. These results should provide important information regarding the biosynthetic basis of moenomycin antibiotics.

中文翻译：

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放线菌teichomyceticus TchmY的晶体结构。

Moenomycin型抗生素是磷酸糖脂，以其独特的作用方式而著称，并已证明可用于动物营养。所述基因簇tchm从游动放线替考霉素游动和MOE从链霉菌是已知moenomycin-生物合成途径的一个有限数量之间。大多数基因在tchm有在同行萌集群，除了tchmy和tchmz，其功能仍然未知。序列分析表明TchmY属于类异戊二烯酶C2样超家族，可作为异戊二烯环化酶。有人提出，该酶参与潮霉素中的美诺霉素链的末端环化，从而导致美诺霉素异构体的丁香酚链。在此，重组TchmY蛋白在大肠杆菌中表达，并通过SIRAS解析其晶体结构。进行结构分析和与其他异戊二烯环化酶的比较。TchmY的整体折叠由（α/α）₆桶组成，并且在中央室中发现了潜在的底物结合袋。这些结果应提供有关莫能霉素抗生素的生物合成基础的重要信息。