T
T. Krojer
Researcher at Structural Genomics Consortium
Publications - 148
Citations - 4678
T. Krojer is an academic researcher from Structural Genomics Consortium. The author has contributed to research in topics: Deposition (chemistry) & Crystal structure. The author has an hindex of 33, co-authored 144 publications receiving 3705 citations. Previous affiliations of T. Krojer include University of Oxford & Max Planck Society.
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Journal ArticleDOI
Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
TL;DR: The crystal structure of DegP, a widely conserved heat shock protein that combines refolding and proteolytic activities, is solved and the chaperone conformation is solved, in which substrate binding in addition to catalysis is abolished.
Journal ArticleDOI
Structural basis for the regulated protease and chaperone function of DegP
TL;DR: The molecular mechanisms underlying the regulated protease and chaperone function of DegP from Escherichia coli are described and it is shown that binding of misfolded proteins transforms hexameric DegP into large, catalytically active 12-meric and 24-meric multimers.
Journal ArticleDOI
Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease.
Alice Douangamath,D. Fearon,P. Gehrtz,T. Krojer,Petra Lukacik,C. David Owen,Efrat Resnick,Claire Strain-Damerell,A. Aimon,Péter Ábrányi-Balogh,José Brandão-Neto,Anna Carbery,Gemma Davison,Alexandre Dias,Thomas D. Downes,Louise Dunnett,Michael Fairhead,James D. Firth,S. Paul Jones,Aaron Keeley,G.M. Keseru,Hanna F. Klein,Mathew P. Martin,Martin E.M. Noble,Peter O'Brien,A.J. Powell,Rambabu N. Reddi,R. Skyner,M. Snee,Michael J. Waring,Conor Wild,Nir London,Frank von Delft,Martin A. Walsh +33 more
TL;DR: A large-scale screen of electrophile and non-covalent fragments is performed through a combined mass spectrometry and X-ray approach against the SARS-CoV-2 main protease, one of two cysteine viral proteases essential for viral replication.
Journal ArticleDOI
Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.
Grazyna Kochan,T. Krojer,David Harvey,Roman Fischer,L Chen,M. Vollmar,F. von Delft,Kathryn L. Kavanagh,Matthew A. Brown,Paul Bowness,Paul Wordsworth,Benedikt M. Kessler,Udo Oppermann +12 more
TL;DR: In this paper, the authors determined crystal structures in open and closed states of human endoplasmatic reticulum aminopeptidase 1 (ERAP1), which provided the first snapshots along a catalytic path.
Journal ArticleDOI
Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases.
Peter Canning,Christopher D.O. Cooper,T. Krojer,James W. Murray,Ashley C. W. Pike,Apirat Chaikuad,T. Keates,Chancievan Thangaratnarajah,Viktorija Hojzan,Brian D. Marsden,Opher Gileadi,Stefan Knapp,Frank von Delft,Alex N. Bullock +13 more
TL;DR: The presented data offer a model for the quaternary assembly of this E3 class that supports the bivalent capture of Nrf2 and reveals potential new sites for E3 inhibitor design.