Crystallization and preliminary X-ray diffraction analysis of the protease from Southampton norovirus complexed with a Michael acceptor inhibitor
Crystallization and preliminary X-ray diffraction analysis of the protease from Southampton norovirus complexed with a Michael acceptor inhibitor
Noroviruses are the predominant cause of human epidemic nonbacterial gastroenteritis. Viral replication requires a cysteine protease that cleaves a 200?kDa viral polyprotein into its constituent functional parts. Here, the crystallization of the recombinant protease from the Southampton norovirus is described. Whilst the native crystals were found to diffract only to medium resolution (2.9?Å), cocrystals of an inhibitor complex diffracted X-rays to 1.7?Å resolution. The polypeptide inhibitor (Ac-EFQLQ-propenyl ethyl ester) possesses an amino-acid sequence designed to match the substrate specificity of the enzyme, but was synthesized with a reactive Michael acceptor group at the C-terminal end.
1544-1548
Hussey, R.J.
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Coates, L.
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Gill, R.S.
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Wright, J. Neville
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Sarwar, M.
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Coker, S.
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Erskine, P.T.
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Cooper, J.B.
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Wood, S.P.
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Clarke, I.N.
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Lambden, P.R.
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Broadbridge, R.
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Shoolingin-Jordan, P.M.
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1 November 2010
Hussey, R.J.
ec7e1411-0b64-4b0a-a2c8-e316fafee567
Coates, L.
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Gill, R.S.
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Wright, J. Neville
e53ee4b9-10f5-4365-a9f2-5a7b0eacd86d
Sarwar, M.
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Coker, S.
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Erskine, P.T.
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Cooper, J.B.
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Wood, S.P.
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Clarke, I.N.
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Lambden, P.R.
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Broadbridge, R.
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Shoolingin-Jordan, P.M.
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Hussey, R.J., Coates, L., Gill, R.S., Wright, J. Neville, Sarwar, M., Coker, S., Erskine, P.T., Cooper, J.B., Wood, S.P., Clarke, I.N., Lambden, P.R., Broadbridge, R. and Shoolingin-Jordan, P.M.
(2010)
Crystallization and preliminary X-ray diffraction analysis of the protease from Southampton norovirus complexed with a Michael acceptor inhibitor.
Acta Crystallographica Section F: Structural Biology Communications, 66 (11), .
(doi:10.1107/S1744309110039059).
(PMID:21045318)
Abstract
Noroviruses are the predominant cause of human epidemic nonbacterial gastroenteritis. Viral replication requires a cysteine protease that cleaves a 200?kDa viral polyprotein into its constituent functional parts. Here, the crystallization of the recombinant protease from the Southampton norovirus is described. Whilst the native crystals were found to diffract only to medium resolution (2.9?Å), cocrystals of an inhibitor complex diffracted X-rays to 1.7?Å resolution. The polypeptide inhibitor (Ac-EFQLQ-propenyl ethyl ester) possesses an amino-acid sequence designed to match the substrate specificity of the enzyme, but was synthesized with a reactive Michael acceptor group at the C-terminal end.
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Published date: 1 November 2010
Identifiers
Local EPrints ID: 173319
URI: http://eprints.soton.ac.uk/id/eprint/173319
ISSN: 2053-230X
PURE UUID: 785091c0-fd31-4e58-87d5-6ee60bd616b8
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Date deposited: 03 Feb 2011 11:14
Last modified: 14 Mar 2024 02:32
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Contributors
Author:
R.J. Hussey
Author:
L. Coates
Author:
R.S. Gill
Author:
J. Neville Wright
Author:
M. Sarwar
Author:
S. Coker
Author:
P.T. Erskine
Author:
J.B. Cooper
Author:
S.P. Wood
Author:
P.R. Lambden
Author:
R. Broadbridge
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