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

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10.1107/S2053230X20011814

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

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.",

keywords = "Neutron diffraction, SARS-CoV-2, X-ray diffraction",

author = "Kneller, \{Daniel W.\} and Gwyndalyn Phillips and Andrey Kovalevsky and Leighton Coates",

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doi = "10.1107/S2053230X20011814",

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T1 - Room-temperature neutron and X-ray data collection of 3CL Mpro from SARS-CoV-2

AU - Kneller, Daniel W.

AU - Phillips, Gwyndalyn

AU - Kovalevsky, Andrey

AU - Coates, Leighton

PY - 2020/10/1

Y1 - 2020/10/1

N2 - 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.

AB - 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.

KW - Neutron diffraction

KW - SARS-CoV-2

KW - X-ray diffraction

UR - https://www.scopus.com/pages/publications/85092561798

U2 - 10.1107/S2053230X20011814

DO - 10.1107/S2053230X20011814

M3 - Article

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AN - SCOPUS:85092561798

SN - 2053-230X

VL - 76

SP - 483

EP - 487

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

ER -

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

Abstract

Keywords

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