Room-temperature neutron and X-ray data collection of 3CL Mpro from SARS-CoV-2

Daniel W. Kneller; Gwyndalyn Phillips; Andrey Kovalevsky; Leighton Coates

doi:10.1107/S2053230X20011814

Room-temperature neutron and X-ray data collection of 3CL M^pro from SARS-CoV-2

Daniel W. Kneller, Gwyndalyn Phillips, Andrey Kovalevsky, Leighton Coates

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

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 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.

Original language	English
Pages (from-to)	483-487
Number of pages	5
Journal	Acta Crystallographica Section F:Structural Biology Communications
Volume	76
DOIs	https://doi.org/10.1107/S2053230X20011814
State	Published - Oct 1 2020

Keywords

Neutron diffraction
SARS-CoV-2
X-ray diffraction

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1107/S2053230X20011814

Cite this

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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.",

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KW - X-ray diffraction

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