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-Structure paper
タイトル | Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex. |
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ジャーナル・号・ページ | Science, Vol. 368, Issue 6489, Page 424-427, Year 2020 |
掲載日 | 2020年4月24日 |
著者 | Gyunghoon Kang / Alexander T Taguchi / JoAnne Stubbe / Catherine L Drennan / |
PubMed 要旨 | 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 ...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, α and β. Because of the transient subunit association, an atomic resolution structure of an active α2β2 RNR complex has been elusive. We used a doubly substituted β2, E52Q/(2,3,5)-trifluorotyrosine122-β2, to trap wild-type α2 in a long-lived α2β2 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. |
リンク | Science / PubMed:32217749 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.6 Å |
構造データ | EMDB-21540, PDB-6w4x: |
化合物 | ChemComp-TTP: ChemComp-MG: ChemComp-GDP: ChemComp-FEO: ChemComp-HOH: |
由来 |
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キーワード | OXIDOREDUCTASE / complex |