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DOI | 10.1126/science.aba6794 |
Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex | |
Kang G.; Taguchi A.T.; Stubbe J.; Drennan C.L. | |
发表日期 | 2020 |
ISSN | 0036-8075 |
起始页码 | 424 |
结束页码 | 427 |
卷号 | 368期号:6489 |
英文摘要 | Ribonucleotide reductases (RNRs) are a diverse family of enzymes that are alone capable of generating 2′-deoxynucleotides de novo and are thus critical in DNA biosynthesis and repair. The nucleotide reduction reaction in all RNRs requires the generation of a transient active site thiyl radical, and in class I RNRs, this process involves a long-range radical transfer between two subunits, a and b. Because of the transient subunit association, an atomic resolution structure of an active a2b2 RNR complex has been elusive. We used a doubly substituted b2, E52Q/(2,3,5)-trifluorotyrosine122-b2, to trap wild-type a2 in a long-lived a2b2 complex. We report the structure of this complex by means of cryo–electron microscopy to 3.6-angstrom resolution, allowing for structural visualization of a 32-angstrom-long radical transfer pathway that affords RNR activity. Copyright © 2020 The Authors, |
关键词 | ribonucleotide reductaseDNAenzymeenzyme activityradicalArticlebeta sheetbinding sitecatalysiscryoelectron microscopyenzyme active siteenzyme activityenzyme bindingenzyme conformationenzyme structureenzyme subunitnonhumanpriority journalsignal transduction |
语种 | 英语 |
来源机构 | Science |
文献类型 | 期刊论文 |
条目标识符 | http://gcip.llas.ac.cn/handle/2XKMVOVA/133551 |
推荐引用方式 GB/T 7714 | Kang G.,Taguchi A.T.,Stubbe J.,et al. Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex[J]. Science,2020,368(6489). |
APA | Kang G.,Taguchi A.T.,Stubbe J.,&Drennan C.L..(2020).Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex.,368(6489). |
MLA | Kang G.,et al."Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex".368.6489(2020). |
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