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Abstract
The replication of SARS-CoV-2 produces two large polyproteins, pp1a and pp1ab, that are inactive until cleavage by the viral chymotrypsin-like cysteine protease enzyme (3CL Mpro) into a series of smaller functional proteins. At the heart of 3CL Mpro is an unusual catalytic dyad formed by the side chains of His41 and Cys145 and a coordinated water molecule. The catalytic mechanism by which the enzyme operates is still unknown, as crucial information on the protonation states within the active site is unclear. To experimentally determine the protonation states of the catalytic site and of the other residues in the substrate-binding cavity, and to visualize the hydrogen-bonding networks throughout the enzyme, room-temperature neutron and X-ray data were collected from a large H/D-exchanged crystal of ligand-free (apo) 3CL Mpro.
Highlights
COVID-19 is a global pandemic that is causing worldwide disruption to travel, economic activity and social life (Zhou et al, 2020; Wu et al, 2020a,b; Coronaviridae Study Group of the International Committee on Taxonomy of Viruses, 2020)
The virus is composed of around 28 proteins that can be broken down into two main classes: nonstructural proteins (NSPs) that are typically involved in viral replication and structural proteins that are involved in forming the structure of the virus
maltosebinding protein (MBP) is followed by the the SARS-CoV-2 NSP4-NSP5 autoprocessing site SAVLQ#SGFRK and 3CL Mpro is followed by the human rhinovirus 3C protease (HRV 3C) cleavage site SGVTFQ#GP
Summary
COVID-19 is a global pandemic that is causing worldwide disruption to travel, economic activity and social life (Zhou et al, 2020; Wu et al, 2020a,b; Coronaviridae Study Group of the International Committee on Taxonomy of Viruses, 2020). Based on earlier studies of SARS-CoV 3CL Mpro, domain III plays an essential role in the protease function as the monomeric enzyme is not catalytically active (Hsu et al, 2005).
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