1lvm
From Proteopedia
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| , resolution 1.80Å | |||||||
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| Ligands: | |||||||
| Related: | 1LVB
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALYTICALLY ACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH PRODUCT
Overview
Because of its stringent sequence specificity, the 3C-type protease from tobacco etch virus (TEV) is frequently used to remove affinity tags from recombinant proteins. It is unclear, however, exactly how TEV protease recognizes its substrates with such high selectivity. The crystal structures of two TEV protease mutants, inactive C151A and autolysis-resistant S219D, have now been solved at 2.2- and 1.8-A resolution as complexes with a substrate and product peptide, respectively. The enzyme does not appear to have been perturbed by the mutations in either structure, and the modes of binding of the product and substrate are virtually identical. Analysis of the protein-ligand interactions helps to delineate the structural determinants of substrate specificity and provides guidance for reengineering the enzyme to further improve its utility for biotechnological applications.
About this Structure
1LVM is a Protein complex structure of sequences from Tobacco etch virus. Full crystallographic information is available from OCA.
Reference
Structural basis for the substrate specificity of tobacco etch virus protease., Phan J, Zdanov A, Evdokimov AG, Tropea JE, Peters HK 3rd, Kapust RB, Li M, Wlodawer A, Waugh DS, J Biol Chem. 2002 Dec 27;277(52):50564-72. Epub 2002 Oct 10. PMID:12377789
Page seeded by OCA on Sun Mar 30 22:08:03 2008
