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Crystallization and preliminary X-ray diffraction analysis of the protease from Southampton norovirus complexed with a Michael acceptor inhibitor

Record type: Article

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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Citation

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), pp. 1544-1548. (doi:10.1107/S1744309110039059). (PMID:21045318).

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Published date: 1 November 2010

Identifiers

Local EPrints ID: 173319
URI: http://eprints.soton.ac.uk/id/eprint/173319
ISSN: 1744-3091
PURE UUID: 785091c0-fd31-4e58-87d5-6ee60bd616b8

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Date deposited: 03 Feb 2011 11:14
Last modified: 18 Jul 2017 12:13

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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: I.N. Clarke
Author: P.R. Lambden
Author: R. Broadbridge

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