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Room‐temperature neutron and X‐ray data collection of 3CL M pro from SARS‐CoV‐2
Author(s) -
Kneller Daniel W.,
Phillips Gwyndalyn,
Kovalevsky Andrey,
Coates Leighton
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20011814
Subject(s) - covid-19 , neutron , data collection , physics , nuclear physics , radiochemistry , virology , chemistry , medicine , statistics , outbreak , mathematics , pathology , infectious disease (medical specialty) , disease
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 M pro ) into a series of smaller functional proteins. At the heart of 3CL M pro 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 M pro .