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Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser.

Journal article
Authors Lars Redecke
Karol Nass
Daniel P DePonte
Thomas A White
Dirk Rehders
Anton Barty
Francesco Stellato
Mengning Liang
Thomas R M Barends
Sébastien Boutet
Garth J Williams
Marc Messerschmidt
M Marvin Seibert
Andrew Aquila
David Arnlund
Sasa Bajt
Torsten Barth
Michael J Bogan
Carl Caleman
Tzu-Chiao Chao
R Bruce Doak
Holger Fleckenstein
Matthias Frank
Raimund Fromme
Lorenzo Galli
Ingo Grotjohann
Mark S Hunter
Linda C Johansson
Stephan Kassemeyer
Gergely Katona
Richard A Kirian
Rudolf Koopmann
Chris Kupitz
Lukas Lomb
Andrew V Martin
Stefan Mogk
Richard Neutze
Robert L Shoeman
Jan Steinbrener
Nicusor Timneanu
Dingjie Wang
Uwe Weierstall
Nadia A Zatsepin
John C H Spence
Petra Fromme
Ilme Schlichting
Michael Duszenko
Christian Betzel
Henry N Chapman
Published in Science (New York, N.Y.)
Volume 339
Issue 6116
Pages 227-30
ISSN 1095-9203
Publication year 2013
Published at Department of Chemistry and Molecular Biology
Pages 227-30
Language en
Keywords Amino Acid Sequence, Animals, Catalytic Domain, Cathepsin B, antagonists & inhibitors, chemistry, Crystallization, Crystallography, X-Ray, Enzyme Precursors, chemistry, Glycosylation, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protozoan Proteins, antagonists & inhibitors, chemistry, Sf9 Cells, Spodoptera, Trypanosoma brucei brucei, enzymology, X-Rays
Subject categories Biochemistry


The Trypanosoma brucei cysteine protease cathepsin B (TbCatB), which is involved in host protein degradation, is a promising target to develop new treatments against sleeping sickness, a fatal disease caused by this protozoan parasite. The structure of the mature, active form of TbCatB has so far not provided sufficient information for the design of a safe and specific drug against T. brucei. By combining two recent innovations, in vivo crystallization and serial femtosecond crystallography, we obtained the room-temperature 2.1 angstrom resolution structure of the fully glycosylated precursor complex of TbCatB. The structure reveals the mechanism of native TbCatB inhibition and demonstrates that new biomolecular information can be obtained by the "diffraction-before-destruction" approach of x-ray free-electron lasers from hundreds of thousands of individual microcrystals.

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