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

被引：4
|
作者：
Hussey, R. J. [2 ]
Coates, L. [3 ]
Gill, R. S. [1 ]
Wright, J. N. [2 ]
Sarwar, M. [2 ]
Coker, S. [1 ]
Erskine, P. T. [1 ]
Cooper, J. B. [1 ]
Wood, S. [1 ]
Clarke, I. N. [4 ]
Lambden, P. R. [4 ]
Broadbridge, R. [5 ]
Shoolingin-Jordan, P. M. [2 ]
机构：
[1] UCL Dept Med, Ctr Amyloidosis & Acute Phase Prot, Lab Prot Crystallog, London NW3 2PF, England
[2] Univ Southampton, Sch Biol Sci, Southampton SO16 7PX, Hants, England
[3] Oak Ridge Natl Lab, Oak Ridge, TN 37831 USA
[4] Southampton Gen Hosp, Univ Med Sch, Div Infect Inflammat & Immun, Mol Microbiol Grp, Southampton SO16 6YD, Hants, England
[5] Peptide Prot Res Ltd, Wickham PO17 5DY, Hants, England
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
基金：
英国惠康基金;
关键词：
3C proteases; noroviruses; Michael acceptors; inhibitor complexes; STRUCTURE-BASED DESIGN; SOLID-PHASE SYNTHESIS; BIOLOGICAL EVALUATION; CLEAVAGE SITES; BINDING SITE; IDENTIFICATION; POLYPROTEIN; EXPRESSION; SEQUENCE; GENOME;
D O I：
10.1107/S1744309110039059
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 A), cocrystals of an inhibitor complex diffracted X-rays to 1.7 A 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.
引用
收藏
页码：1544 / 1548
页数：5
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