Nature Communications (Jan 2020)
In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors
- Karol Nass,
- Lars Redecke,
- M. Perbandt,
- O. Yefanov,
- M. Klinge,
- R. Koopmann,
- F. Stellato,
- A. Gabdulkhakov,
- R. Schönherr,
- D. Rehders,
- J. M. Lahey-Rudolph,
- A. Aquila,
- A. Barty,
- S. Basu,
- R. B. Doak,
- R. Duden,
- M. Frank,
- R. Fromme,
- S. Kassemeyer,
- G. Katona,
- R. Kirian,
- H. Liu,
- I. Majoul,
- J. M. Martin-Garcia,
- M. Messerschmidt,
- R. L. Shoeman,
- U. Weierstall,
- S. Westenhoff,
- T. A. White,
- G. J. Williams,
- C. H. Yoon,
- N. Zatsepin,
- P. Fromme,
- M. Duszenko,
- H. N. Chapman,
- C. Betzel
Affiliations
- Karol Nass
- Center for Free-Electron Laser Science (CFEL), Deutsches Elektronen-Synchrotron DESY
- Lars Redecke
- Joint Laboratory for Structural Biology of Infection and Inflammation, Institute of Biochemistry and Molecular Biology, University of Hamburg, and Institute of Biochemistry, University of Lübeck, at Deutsches Elektronen-Synchrotron (DESY)
- M. Perbandt
- Institute of Biochemistry and Molecular Biology, University of Hamburg, at Deutsches Elektronen-Synchrotron (DESY)
- O. Yefanov
- Center for Free-Electron Laser Science (CFEL), Deutsches Elektronen-Synchrotron DESY
- M. Klinge
- Joint Laboratory for Structural Biology of Infection and Inflammation, Institute of Biochemistry and Molecular Biology, University of Hamburg, and Institute of Biochemistry, University of Lübeck, at Deutsches Elektronen-Synchrotron (DESY)
- R. Koopmann
- Interfaculty Institute of Biochemistry, University of Tübingen
- F. Stellato
- Center for Free-Electron Laser Science (CFEL), Deutsches Elektronen-Synchrotron DESY
- A. Gabdulkhakov
- Institute of Protein Research, Russian Academy of Sciences
- R. Schönherr
- Institute of Biochemistry, University of Lübeck
- D. Rehders
- Joint Laboratory for Structural Biology of Infection and Inflammation, Institute of Biochemistry and Molecular Biology, University of Hamburg, and Institute of Biochemistry, University of Lübeck, at Deutsches Elektronen-Synchrotron (DESY)
- J. M. Lahey-Rudolph
- Center for Free-Electron Laser Science (CFEL), Deutsches Elektronen-Synchrotron DESY
- A. Aquila
- Center for Free-Electron Laser Science (CFEL), Deutsches Elektronen-Synchrotron DESY
- A. Barty
- Center for Free-Electron Laser Science (CFEL), Deutsches Elektronen-Synchrotron DESY
- S. Basu
- Department of Chemistry and Biochemistry, Arizona State University
- R. B. Doak
- Department of Physics, Arizona State University
- R. Duden
- Institute of Biology, University of Lübeck
- M. Frank
- Biology and Biotechnology Division, Physical & Life Sciences Directorate, Lawrence Livermore National Laboratory
- R. Fromme
- Department of Chemistry and Biochemistry, Arizona State University
- S. Kassemeyer
- Max-Planck-Institute for Medical Research
- G. Katona
- Department of Chemistry and Molecular Biology, University of Gothenburg
- R. Kirian
- Department of Chemistry and Biochemistry, Arizona State University
- H. Liu
- Department of Physics, Arizona State University
- I. Majoul
- Institute of Biology, University of Lübeck
- J. M. Martin-Garcia
- Center for Applied Structural Discovery (CASD), Biodesign Institute, Arizona State University
- M. Messerschmidt
- LCLS, SLAC National Accelerator Laboratory
- R. L. Shoeman
- Max-Planck-Institute for Medical Research
- U. Weierstall
- Department of Physics, Arizona State University
- S. Westenhoff
- Department of Chemistry and Molecular Biology, University of Gothenburg
- T. A. White
- Center for Free-Electron Laser Science (CFEL), Deutsches Elektronen-Synchrotron DESY
- G. J. Williams
- LCLS, SLAC National Accelerator Laboratory
- C. H. Yoon
- Center for Free-Electron Laser Science (CFEL), Deutsches Elektronen-Synchrotron DESY
- N. Zatsepin
- Department of Physics, Arizona State University
- P. Fromme
- Department of Chemistry and Biochemistry, Arizona State University
- M. Duszenko
- Institute of Neurophysiology, University of Tübingen
- H. N. Chapman
- Center for Free-Electron Laser Science (CFEL), Deutsches Elektronen-Synchrotron DESY
- C. Betzel
- Institute of Biochemistry and Molecular Biology, University of Hamburg, at Deutsches Elektronen-Synchrotron (DESY)
- DOI
- https://doi.org/10.1038/s41467-020-14484-w
- Journal volume & issue
-
Vol. 11,
no. 1
pp. 1 – 13
Abstract
Trypanosoma brucei inosine-5′-monophosphate dehydrogenase (IMPDH) is an enzyme in the guanine nucleotide biosynthesis pathway and of interest as a drug target. Here the authors present the 2.8 Å room temperature structure of TbIMPDH determined by utilizing X-ray free-electron laser radiation and crystals that were grown in insect cells and find that ATP and GMP are bound at the canonical sites of the Bateman domains.
