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Structure of a ribonucleotide reductase R2 protein radical

Lebrette, Hugo ; Srinivas, Vivek ; John, Juliane ; Aurelius, Oskar LU ; Kumar, Rohit ; Lundin, Daniel ; Brewster, Aaron S. ; Bhowmick, Asmit ; Sirohiwal, Abhishek and Kim, In Sik , et al. (2023) In Science 382(6666). p.109-113
Abstract

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 it to the translocation path, with structural changes propagating to the surface where the protein interacts with the catalytic R1 subunit. Restructuring of the hydrogen bond network, including a notably short O–O interaction of 2.41 angstroms,... (More)

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 it to the translocation path, with structural changes propagating to the surface where the protein interacts with the catalytic R1 subunit. Restructuring of the hydrogen bond network, including a notably short O–O interaction of 2.41 angstroms, likely tunes and gates the radical during PCET. These structural results help explain radical handling and mobilization in RNR and have general implications for radical transfer in proteins.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Science
volume
382
issue
6666
pages
5 pages
publisher
American Association for the Advancement of Science (AAAS)
external identifiers
  • pmid:37797025
  • scopus:85174847670
ISSN
0036-8075
DOI
10.1126/science.adh8160
language
English
LU publication?
yes
id
9dd96a5f-336b-4809-8177-c430ef92c115
date added to LUP
2023-12-11 14:21:45
date last changed
2024-04-24 07:49:47
@article{9dd96a5f-336b-4809-8177-c430ef92c115,
  abstract     = {{<p>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 it to the translocation path, with structural changes propagating to the surface where the protein interacts with the catalytic R1 subunit. Restructuring of the hydrogen bond network, including a notably short O–O interaction of 2.41 angstroms, likely tunes and gates the radical during PCET. These structural results help explain radical handling and mobilization in RNR and have general implications for radical transfer in proteins.</p>}},
  author       = {{Lebrette, Hugo and Srinivas, Vivek and John, Juliane and Aurelius, Oskar and Kumar, Rohit and Lundin, Daniel and Brewster, Aaron S. and Bhowmick, Asmit and Sirohiwal, Abhishek and Kim, In Sik and Gul, Sheraz and Pham, Cindy and Sutherlin, Kyle D. and Simon, Philipp and Butryn, Agata and Aller, Pierre and Orville, Allen M. and Fuller, Franklin D. and Alonso-Mori, Roberto and Batyuk, Alexander and Sauter, Nicholas K. and Yachandra, Vittal K. and Yano, Junko and Kaila, Ville R.I. and Sjöberg, Britt Marie and Kern, Jan and Roos, Katarina and Högbom, Martin}},
  issn         = {{0036-8075}},
  language     = {{eng}},
  number       = {{6666}},
  pages        = {{109--113}},
  publisher    = {{American Association for the Advancement of Science (AAAS)}},
  series       = {{Science}},
  title        = {{Structure of a ribonucleotide reductase R2 protein radical}},
  url          = {{http://dx.doi.org/10.1126/science.adh8160}},
  doi          = {{10.1126/science.adh8160}},
  volume       = {{382}},
  year         = {{2023}},
}