Crystal Structure of Tobacco Etch Virus Protease Shows the Protein C Terminus Bound within the Active Site

Nunn, Christine M. and Jeeves, Mark and Cliff, Matthew J. and Urquhart, Gillian T. and George, Roger R. and Chao, Luke H. and Tscuchia, Yugo and Djordjevic, Snezana (2005) Crystal Structure of Tobacco Etch Virus Protease Shows the Protein C Terminus Bound within the Active Site. Journal of Molecular Biology, 350 (1). pp. 145-155. ISSN 0022-2836

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Official URL: http://dx.doi.org/10.1016/j.jmb.2005.04.013

Abstract

Tobacco etch virus (TEV) protease is a cysteine protease exhibiting stringent sequence specificity. The enzyme is widely used in biotechnology for the removal of the affinity tags from recombinant fusion proteins. Crystal structures of two TEV protease mutants as complexes with a substrate and a product peptide provided the first insight into the mechanism of substrate specificity of this enzyme. We now report a 2.7 A˚ crystal structure of a full-length inactive C151A mutant protein crystallised in the absence of peptide. The structure reveals the C terminus of the protease bound to the active site. In addition, we determined dissociation constants of TEV protease substrate and product peptides using isothermal titration calorimetry for various forms of this enzyme. Data suggest that TEV protease could be inhibited by the peptide product of autolysis. Separate modes of recognition for native substrates and the site of TEV protease self-cleavage are proposed.

Item Type: Article
Uncontrolled Keywords: Tobacco etch virus (TEV) protease
Subjects: 500 Natural Sciences and Mathemetics > 540 Chemistry & allied sciences
500 Natural Sciences and Mathemetics > 570 Life sciences; biology
Department: School of Human Sciences
Depositing User: Christine Nunn
Date Deposited: 03 Aug 2015 10:41
Last Modified: 21 Aug 2015 08:27
URI: http://repository.londonmet.ac.uk/id/eprint/735

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