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Time-resolved crystallography captures light-driven DNA repair.
Christou, Nina-Eleni; Apostolopoulou, Virginia; Melo, Diogo V M; Ruppert, Matthias; Fadini, Alisia; Henkel, Alessandra; Sprenger, Janina; Oberthuer, Dominik; Günther, Sebastian; Pateras, Anastasios; Rahmani Mashhour, Aida; Yefanov, Oleksandr M; Galchenkova, Marina; Reinke, Patrick Y A; Kremling, Viviane; Scheer, T Emilie S; Lange, Esther R; Middendorf, Philipp; Schubert, Robin; De Zitter, Elke; Lumbao-Conradson, Koya; Herrmann, Jonathan; Rahighi, Simin; Kunavar, Ajda; Beale, Emma V; Beale, John H; Cirelli, Claudio; Johnson, Philip J M; Dworkowski, Florian; Ozerov, Dmitry; Bertrand, Quentin; Wranik, Maximilian; Bacellar, Camila; Bajt, Sasa; Wakatsuki, Soichi; Sellberg, Jonas A; Huse, Nils; Turk, Dusan; Chapman, Henry N; Lane, Thomas J.
Affiliation
  • Christou NE; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Apostolopoulou V; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Melo DVM; The Hamburg Centre for Ultrafast Imaging, Luruper Chaussee 149, 22761 Hamburg, Germany.
  • Ruppert M; European XFEL GmbH, Holzkoppel 4, 22869 Schenefeld, Germany.
  • Fadini A; Institute for Nanostructure and Solid-State Physics, CFEL Universität Hamburg, Luruper Chaussee 149, 22761 Hamburg, Germany.
  • Henkel A; Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.
  • Sprenger J; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Oberthuer D; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Günther S; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Pateras A; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Rahmani Mashhour A; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Yefanov OM; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Galchenkova M; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Reinke PYA; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Kremling V; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Scheer TES; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Lange ER; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Middendorf P; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Schubert R; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • De Zitter E; European XFEL GmbH, Holzkoppel 4, 22869 Schenefeld, Germany.
  • Lumbao-Conradson K; Université Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale, 38000 Grenoble, France.
  • Herrmann J; Linac Coherent Light Source, SLAC National Accelerator Laboratory, 2575 Sand Hill Rd, Menlo Park, CA 94025, USA.
  • Rahighi S; Department of Structural Biology, Stanford University, 318 Campus Drive West, Stanford, CA 94305-5151, USA.
  • Kunavar A; Department of Structural Biology, Stanford University, 318 Campus Drive West, Stanford, CA 94305-5151, USA.
  • Beale EV; Laboratory for Fluid Dynamics and Thermodynamics, Faculty of Mechanical Engineering, University of Ljubljana, Askerceva 6, 1000 Ljubljana, Slovenia.
  • Beale JH; Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.
  • Cirelli C; Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.
  • Johnson PJM; Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.
  • Dworkowski F; Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.
  • Ozerov D; Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.
  • Bertrand Q; Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.
  • Wranik M; Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.
  • Bacellar C; Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.
  • Bajt S; Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.
  • Wakatsuki S; Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
  • Sellberg JA; The Hamburg Centre for Ultrafast Imaging, Luruper Chaussee 149, 22761 Hamburg, Germany.
  • Huse N; Department of Structural Biology, Stanford University, 318 Campus Drive West, Stanford, CA 94305-5151, USA.
  • Turk D; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, 2575 Sand Hill Rd, Menlo Park, CA 94025, USA.
  • Chapman HN; Biomedical and X-ray Physics, Department of Applied Physics, AlbaNova University Center, KTH Royal Institute of Technology, S-106 91 Stockholm, Sweden.
  • Lane TJ; The Hamburg Centre for Ultrafast Imaging, Luruper Chaussee 149, 22761 Hamburg, Germany.
Science ; 382(6674): 1015-1020, 2023 12.
Article in En | MEDLINE | ID: mdl-38033070
Photolyase is an enzyme that uses light to catalyze DNA repair. To capture the reaction intermediates involved in the enzyme's catalytic cycle, we conducted a time-resolved crystallography experiment. We found that photolyase traps the excited state of the active cofactor, flavin adenine dinucleotide (FAD), in a highly bent geometry. This excited state performs electron transfer to damaged DNA, inducing repair. We show that the repair reaction, which involves the lysis of two covalent bonds, occurs through a single-bond intermediate. The transformation of the substrate into product crowds the active site and disrupts hydrogen bonds with the enzyme, resulting in stepwise product release, with the 3' thymine ejected first, followed by the 5' base.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Deoxyribodipyrimidine Photo-Lyase Language: En Journal: Science Year: 2023 Type: Article Affiliation country: Germany
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Deoxyribodipyrimidine Photo-Lyase Language: En Journal: Science Year: 2023 Type: Article Affiliation country: Germany