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学科主题: Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
题名: Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis
作者: [Zhang, Huaidong ; Chen, Jie ; Wang, Hua ; Yan, Yunjun ; Zhang, Houjin] Minist Educ, Key Lab Mol Biophys, Wuhan 430074, Hubei, Peoples R China ; [Zhang, Huaidong ; Chen, Jie ; Wang, Hua ; Yan, Yunjun ; Zhang, Houjin] Huazhong Univ Sci & Technol, Dept Biotechnol, Coll Life Sci & Technol, Wuhan 430074, Hubei, Peoples R China ; [Xie, Yunchang ; Ju, Jianhua] Chinese Acad Sci, South China Sea Inst Oceanol, CAS Key Lab Marine Bioresources Sustainable Utili, Guangzhou 510301, Guangdong, Peoples R China
通讯作者: yanyunjun@hust.edu.cn ; hjzhang@hust.edu.cn
关键词: Himastatin ; HmtT ; HmtN ; Cytochrome P450 ; Crystal structure
刊名: FEBS LETTERS
发表日期: 2013
卷: 587, 期:11, 页:1675-1680
部门归属: LMB
资助者: This research was financially supported by National Natural Science Foundation of China (No. 31000326 and 20872152), National Key Basic Research Program of China (No. 2013CB933900) and Fundamental Research Funds for the Central Universities (No. 01-18170005). We thank Zengqiang Gao and Defeng Li for technical assistance and helpful discussion. The diffraction data were collected on beam-line BL17U at SSRF and at the Institute of Biophysics, Chinese Academy of Sciences.
摘要: 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. (c) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
语种: 英语
原文出处: 查看原文
WOS记录号: WOS:000319445900015
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内容类型: 期刊论文
URI标识: http://ir.scsio.ac.cn/handle/344004/11017
Appears in Collections:中科院海洋生物资源可持续利用重点实验室_期刊论文

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[Zhang, Huaidong; Chen, Jie; Wang, Hua; Yan, Yunjun; Zhang, Houjin] Minist Educ, Key Lab Mol Biophys, Wuhan 430074, Hubei, Peoples R China; [Zhang, Huaidong; Chen, Jie; Wang, Hua; Yan, Yunjun; Zhang, Houjin] Huazhong Univ Sci & Technol, Dept Biotechnol, Coll Life Sci & Technol, Wuhan 430074, Hubei, Peoples R China; [Xie, Yunchang; Ju, Jianhua] Chinese Acad Sci, South China Sea Inst Oceanol, CAS Key Lab Marine Bioresources Sustainable Utili, Guangzhou 510301, Guangdong, Peoples R China.Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis,FEBS LETTERS,2013,587(11):1675-1680
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