10.1002/anie.201808189
Angewandte Chemie International Edition
COMMUNICATION
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Further evidence such as competitive binding with the chaperone,
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within the binding pocket is an important feature that controls
hClpP proteolytic activity as well as D9 binding, presumably via p-
stacking interactions triggered by electronic effects of crucial
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activated upon a tight and close binding of ClpX. D9 is
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driven global conformational changes. Especially in the context of
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Keywords: Human ClpP • Proteolysis • Activation •
Crystallography
[25]
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Acknowledgements
We
are
grateful for funding
from the
Deutsche
Forschungsgemeinschaft (ClpP SI1096/8-1, SFB1035, CIPSM to
S.A.S.; SCHN1273/6-1 and CIPSM to S.S.). M.S. was supported
by the German National Merit Foundation and the TUM Graduate
School. LmClpP2 was kindly provided by Dr. Maria Dahmen. We
thank Susann Badmann, Joel Fauser, Anja Fux, Carolin Gleißner,
Sabine Helmrath, Elisabeth Kleber, Katharina Lamm, Mona Wolff,
Karolina Koch, Jacqueline Kissel, and Linda Nguyen for help with
experiments. We also thank the European Synchrotron Radiation
Facility (ESRF) for beamtime and the staff of beamline ID23-2 for
setting up the beamline for data collection.
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