Structure of a ribonucleotide reductase R2 protein radical.
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ABSTRACT:
SUBMITTER: Lebrette H
PROVIDER: S-EPMC7615503 | biostudies-literature | 2023 Oct
REPOSITORIES: biostudies-literature
Publications
Structure of a ribonucleotide reductase R2 protein radical.
Lebrette Hugo H Srinivas Vivek V John Juliane J Aurelius Oskar O Kumar Rohit R Lundin Daniel D Brewster Aaron S AS Bhowmick Asmit A Sirohiwal Abhishek A Kim In-Sik IS Gul Sheraz S Pham Cindy C Sutherlin Kyle D KD Simon Philipp P Butryn Agata A Aller Pierre P Orville Allen M AM Fuller Franklin D FD Alonso-Mori Roberto R Batyuk Alexander A Sauter Nicholas K NK Yachandra Vittal K VK Yano Junko J Kaila Ville R I VRI Sjöberg Britt-Marie BM Kern Jan J Roos Katarina K Högbom Martin M
Science (New York, N.Y.) 20231005 6666
Aerobic ribonucleotide reductases (RNRs) initiate synthesis of DNA building blocks by generating a free radical within the R2 subunit; the radical is subsequently shuttled to the catalytic R1 subunit through proton-coupled electron transfer (PCET). We present a high-resolution room temperature structure of the class Ie R2 protein radical captured by x-ray free electron laser serial femtosecond crystallography. The structure reveals conformational reorganization to shield the radical and connect ...[more]
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