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

journal contribution
posted on 2023-06-09, 04:36 authored by R J Hussey, L Coates, R S Gill, J N Wright, M Sarwar, S Coker, P T Erskine, J B Cooper, S Wood, I N Clarke, P R Lambden, R Broadbridge, P M Shoolingin-Jordan
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.

History

Publication status

  • Published

Journal

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

ISSN

1744-3091

Publisher

International Union of Crystallography

Issue

11

Volume

66

Page range

1544-1548

Department affiliated with

  • Chemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2017-01-09

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