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Statistical crystallography reveals an allosteric network in SARS-CoV-2 Mpro
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Journal Article
Statistical crystallography reveals an allosteric network in SARS-CoV-2 Mpro
2026
Overview
To interpret and transmit biological signals, proteins use correlated motions. Experimental determination of these dynamics and the structural distributions they generate remains a key challenge. Here, using 1146 crystal structures of the main protease (M
pro
) from SARS-CoV-2, we were able to infer a model of the enzyme’s structural fluctuations. M
pro
is regulated by concentration, becoming enzymatically active after forming a homodimer. To understand the structural changes that enable dimerization to activate catalysis, we employed our model, predicting which regions of the dimerization domain are structurally correlated with the active site. Mutations at these positions, expected to disrupt catalysis, resulted in a dramatic reduction in activity in one case, a mild effect in the second, and none in the third. Additional crystallography and biophysical experiments provide a mechanistic explanation for these results. Our work suggests that a statistical crystallography, in which numerous crystallographic datasets are analyzed, can reveal the structural fluctuations of protein native states and help uncover their biological function.
Using the small differences across 1146 crystal structures we collected of the SARS-CoV-2 main protease, we map correlated atomic fluctuations to predict and experimentally confirm a functional allosteric network.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
