Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography

Daniel W. Kneller, Gwyndalyn Phillips, Hugh M. O’Neill, Robert Jedrzejczak, Lucy Stols, Paul Langan, Andrzej Joachimiak, Leighton Coates () and Andrey Kovalevsky ()
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Daniel W. Kneller: Oak Ridge National Laboratory
Gwyndalyn Phillips: Oak Ridge National Laboratory
Hugh M. O’Neill: Oak Ridge National Laboratory
Robert Jedrzejczak: University of Chicago
Lucy Stols: University of Chicago
Paul Langan: Oak Ridge National Laboratory
Andrzej Joachimiak: University of Chicago
Leighton Coates: Oak Ridge National Laboratory
Andrey Kovalevsky: Oak Ridge National Laboratory

Nature Communications, 2020, vol. 11, issue 1, 1-6

Abstract: Abstract The COVID-19 disease caused by the SARS-CoV-2 coronavirus has become a pandemic health crisis. An attractive target for antiviral inhibitors is the main protease 3CL Mpro due to its essential role in processing the polyproteins translated from viral RNA. Here we report the room temperature X-ray structure of unliganded SARS-CoV-2 3CL Mpro, revealing the ligand-free structure of the active site and the conformation of the catalytic site cavity at near-physiological temperature. Comparison with previously reported low-temperature ligand-free and inhibitor-bound structures suggest that the room temperature structure may provide more relevant information at physiological temperatures for aiding in molecular docking studies.

Date: 2020
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DOI: 10.1038/s41467-020-16954-7

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