File(s) not publicly available
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-JordanNoroviruses 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 CommunicationsISSN
1744-3091Publisher
International Union of CrystallographyExternal DOI
Issue
11Volume
66Page range
1544-1548Department affiliated with
- Chemistry Publications
Full text available
- No
Peer reviewed?
- Yes