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Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis
[Zhang, Huaidong; Chen, Jie; Wang, Hua; Yan, Yunjun; Zhang, Houjin] Minist Educ, Key Lab Mol Biophys, Wuhan 430074, Hubei, Peoples R China; 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; yanyunjun@hust.edu.cn; hjzhang@hust.edu.cn
2013
Source PublicationFEBS LETTERS
ISSN0014-5793
Volume587Issue:11Pages:1675-1680
AbstractHimastatin 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.
DepartmentLMB
KeywordHimastatin Hmtt Hmtn Cytochrome P450 Crystal Structure
Subject AreaBiochemistry & Molecular Biology ; Biophysics ; Cell Biology
Funding OrganizationThis 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. ; 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. ; 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. ; 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.
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Language英语
Funding OrganizationThis 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. ; 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. ; 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. ; 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.
WOS IDWOS:000319445900015
Citation statistics
Document Type期刊论文
Identifierhttp://ir.scsio.ac.cn/handle/344004/11017
Collection中科院海洋生物资源可持续利用重点实验室
Corresponding Authoryanyunjun@hust.edu.cn; hjzhang@hust.edu.cn
Recommended Citation
GB/T 7714
[Zhang, Huaidong,Chen, Jie,Wang, Hua,et al. Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis[J]. FEBS LETTERS,2013,587(11):1675-1680.
APA [Zhang, Huaidong.,Chen, Jie.,Wang, Hua.,Yan, Yunjun.,Zhang, Houjin] Minist Educ, Key Lab Mol Biophys, Wuhan 430074, Hubei, Peoples R China.,...&hjzhang@hust.edu.cn.(2013).Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis.FEBS LETTERS,587(11),1675-1680.
MLA [Zhang, Huaidong,et al."Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis".FEBS LETTERS 587.11(2013):1675-1680.
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