Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
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DOI：
10.1126/science.1088493
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发表时间：
2004-01-02
期刊：
影响因子：
56.9
通讯作者：
Drennan, CL
中科院分区：
文献类型：
--
作者：
Berkovitch, F;Nicolet, Y;Drennan, CL
大肠杆菌生物素合酶与S-腺苷-L-甲硫氨酸和脱硫生物素复合物的晶体结构已被确定为3.4埃分辨率。该结构解决了“硫代甲硫氨酸自由基”或“自由基SAM”酶如何使用Fe 4S 4簇和S-腺苷-L-甲硫氨酸来产生有机自由基。生物素合酶催化自由基介导的硫插入脱硫生物素中以形成生物素。该结构的地方之间的Fe 4S 4集群，自由基生成必不可少的基板，和Fe 2S 2集群，假定是硫的来源，与两个集群在前所未有的协调环境。
The crystal structure of biotin synthase from Escherichia coli in complex with S-adenosyl-L-methionine and dethiobiotin has been determined to 3.4 angstrom resolution. This structure addresses how "AdoMet radical" or "radical SAM" enzymes use Fe4S4 clusters and S-adenosyl-L-methionine to generate organic radicals. Biotin synthase catalyzes the radical-mediated insertion of sulfur into dethiobiotin to form biotin. The structure places the substrates between the Fe4S4 cluster, essential for radical generation, and the Fe2S2 cluster, postulated to be the source of sulfur, with both clusters in unprecedented coordination environments.