Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex
Name
nihms-1657035.pdf
Description
Accepted version
Size
2.02 MB
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Unknown
Checksum (MD5)
7d5d704d529ef7895608a5e3d542f421
Author(s)
Kang, Gyunghoon
Taguchi, Alexander T.
Stubbe, JoAnne
Drennan, Catherine L.
Date Issued
April 2020
Journal
Science
Publisher
American Association for the Advancement of Science (AAAS)
Version
Author's final manuscript
Abstract
Copyright © 2020 The Authors, 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.
MIT Department
Howard Hughes Medical Institute
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1126/science.aba6794
