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...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-11, Vol.66 (11), p.1544-1548
Main Authors: Hussey, R. J., Coates, L., Gill, R. S., Wright, J. N., Sarwar, M., Coker, S., Erskine, P. T., Cooper, J. B., Wood, S., Clarke, I. N., Lambden, P. R., Broadbridge, R., Shoolingin-Jordan, P. M.
Format: Article
Language:English
Subjects:
3C proteases
Crystallization
Crystallization Communications
Crystallography, X-Ray
Endopeptidases - chemistry
Endopeptidases - metabolism
inhibitor complexes
Kinetics
Michael acceptors
Norovirus
Norovirus - enzymology
noroviruses
Protease Inhibitors - chemistry
Protease Inhibitors - metabolism
Protein Interaction Domains and Motifs
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Summary: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.
ISSN:1744-3091
1744-3091
2053-230X
DOI:10.1107/S1744309110039059