Room-temperature neutron and X-ray data collection of 3CL Mpro from SARS-CoV-2.
Acta Crystallogr F Struct Biol Commun
; 76(Pt 10): 483-487, 2020 Oct 01.
Article
in English
| MEDLINE | ID: covidwho-817571
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.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Pneumonia, Viral
/
Cysteine Endopeptidases
/
Viral Nonstructural Proteins
/
Coronavirus Infections
/
Betacoronavirus
Limits:
Humans
Language:
English
Journal:
Acta Crystallogr F Struct Biol Commun
Year:
2020
Document Type:
Article
Affiliation country:
S2053230x20011814
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