Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis
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- 作者：Huaidong Zhang ; Jie Chen ; Hua Wang ; Yunchang Xie ; Jianhua Ju ; Yunjun Yan ; Houjin Zhang
- 关键词：NRPS ; non-ribosomal peptide synthetase ; CYP ; cytochrome P450 ; Pip ; piperazic acid ; IPTG ; isopropyl ¦Â-d-1-thiogalactopyranoside ; PEG ; polyethylene glycol ; SSRF ; Shanghai synchrotron radiation facility ; RMSD ; root mean square deviation
- 刊名：FEBS Letters
- 出版年：2013
- 出版时间：5 June, 2013
- 年：2013
- 卷：587
- 期：11
- 页码：1675-1680
- 全文大小：1585 K
文摘
Himastatin is a novel antibiotic featuring a bicyclohexadepsipeptide structure. On the himastatin biosynthesis pathway, three cytochrome P450s (HmtT, HmtN, HmtS) are responsible for the post-tailoring of the cyclohexadepsipeptide backbone. Here we report the crystal structures of HmtT and HmtN. The overall structures of these two proteins are homologous to other cytochrome P450s. However, the exceptionally long F-G loop in HmtT has a highly unusual conformation and extends deep into the active site. As a result, the F/G helices of HmtT are both kinked. In contrast, the F/G helices of HmtN are straight. Also, the F/G helices in HmtT and HmtN take distinctive orientations, which may be a contributing factor for the substrate specificity of these two enzymes.