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Structure of a ribonucleotide reductase R2 protein radical.
Lebrette, Hugo; Srinivas, Vivek; John, Juliane; Aurelius, Oskar; Kumar, Rohit; Lundin, Daniel; Brewster, Aaron S; Bhowmick, Asmit; Sirohiwal, Abhishek; Kim, In-Sik; Gul, Sheraz; Pham, Cindy; Sutherlin, Kyle D; Simon, Philipp; Butryn, Agata; Aller, Pierre; Orville, Allen M; Fuller, Franklin D; Alonso-Mori, Roberto; Batyuk, Alexander; Sauter, Nicholas K; Yachandra, Vittal K; Yano, Junko; Kaila, Ville R I; Sjöberg, Britt-Marie; Kern, Jan; Roos, Katarina; Högbom, Martin.
Afiliación
  • Lebrette H; Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm, Sweden.
  • Srinivas V; Laboratoire de Microbiologie et Génétique Moléculaires, Centre de Biologie Intégrative, CNRS, Université Toulouse III, Toulouse, France.
  • John J; Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm, Sweden.
  • Aurelius O; Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm, Sweden.
  • Kumar R; Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm, Sweden.
  • Lundin D; MAX IV Laboratory, Lund University, Lund, Sweden.
  • Brewster AS; Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm, Sweden.
  • Bhowmick A; Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm, Sweden.
  • Sirohiwal A; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Kim IS; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Gul S; Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Stockholm, Sweden.
  • Pham C; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Sutherlin KD; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Simon P; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Butryn A; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Aller P; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Orville AM; Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, UK.
  • Fuller FD; Research Complex at Harwell, Harwell Science and Innovation Campus, Didcot, UK.
  • Alonso-Mori R; Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, UK.
  • Batyuk A; Research Complex at Harwell, Harwell Science and Innovation Campus, Didcot, UK.
  • Sauter NK; Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, UK.
  • Yachandra VK; Research Complex at Harwell, Harwell Science and Innovation Campus, Didcot, UK.
  • Yano J; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
  • Kaila VRI; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
  • Sjöberg BM; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
  • Kern J; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Roos K; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Högbom M; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Science ; 382(6666): 109-113, 2023 10 06.
Article en En | MEDLINE | ID: mdl-37797025
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, 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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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Ribonucleótido Reductasas / Proteínas Bacterianas / Entomoplasmataceae Idioma: En Revista: Science Año: 2023 Tipo del documento: Article País de afiliación: Suecia
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Ribonucleótido Reductasas / Proteínas Bacterianas / Entomoplasmataceae Idioma: En Revista: Science Año: 2023 Tipo del documento: Article País de afiliación: Suecia