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学科主题: Biochemistry & Molecular Biology ; Biophysics ; Crystallography
题名: Expression, crystallization and preliminary X-ray analysis of McbB, a multifunctional enzyme involved in beta-carboline skeleton biosynthesis
作者: Wang, H ; Zhang, HD ; Mi, YL ; Ju, JH ; Chen, Q ; Zhang, HJ
通讯作者: hjzhang@hust.edu.cn
刊名: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
发表日期: 2014
卷: 70, 页:1402-1405
收录类别: sci
部门归属: [Wang, Hua ; Zhang, Huaidong ; Mi, Yanling ; Zhang, Houjin] Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Hubei, Peoples R China ; [Ju, Jianhua ; Chen, Qi] Chinese Acad Sci, CAS Key Lab Trop Marine Bioresources & Ecol, South China Sea Inst Oceanol Microbiol,Guangdong, South China Sea Inst Oceanol,RNAM Ctr Marine Micr, Guangzhou 510301, Guangdong, Peoples R China
项目归属: LMB
资助者: National Key Basic Research Program of China [2013CB933900]; National Natural Science Foundation of China [31000326]
摘要: beta-Carboline alkaloids (beta Cs), with tricyclic pyrido[3,4-b] indole rings, have important pharmacological and therapeutic value. In the biosynthesis of beta Cs, the Pictet-Spengler (PS) cyclization reaction is responsible for the formation of ring structures. McbB is one of a few enzymes that are known to catalyse PS cyclization. It can also catalyse decarboxylation and oxidation. Here, the expression, crystallization and preliminary data analysis of McbB are reported. The crystals diffracted to 2.10 angstrom resolution and belonged to the monoclinic space group P2(1), with unit-cell parameters a = 66.06, b = 85.48, c = 106.19 angstrom, alpha = 90.00, beta = 106.77, gamma = 90.00 degrees. These results provide a basis for solving the crystal structure and elucidating the catalytic mechanism for McbB.
原文出处: 查看原文
WOS记录号: WOS:000343060200020
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内容类型: 期刊论文
URI标识: http://ir.scsio.ac.cn/handle/344004/10377
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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Wang, H; Zhang, HD; Mi, YL; Ju, JH; Chen, Q; Zhang, HJ.Expression, crystallization and preliminary X-ray analysis of McbB, a multifunctional enzyme involved in beta-carboline skeleton biosynthesis,ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS,2014,70():1402-1405
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