1LVB

CATALYTICALLY INACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH SUBSTRATE

Summary for 1LVB

• Entry DOI: 10.2210/pdb1lvb/pdb
• Related: 1LVM
• Descriptor: CATALYTIC DOMAIN OF THE NUCLEAR INCLUSION PROTEIN A (NIA), OLIGOPEPTIDE SUBSTRATE FOR THE PROTEASE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: beta barrel, protein-peptide complex, chymotrypsin-like cystein protease, viral protein
• Biological source: Tobacco etch virus
• Cellular location: Capsid protein: Virion (Potential): P04517 P04517
• Total number of polymer chains: 4
• Total formula weight: 58512.02

Authors

Phan, J.,Zdanov, A.,Evdokimov, A.G.,Tropea, J.E.,Peters III, H.K.,Kapust, R.B.,Li, M.,Wlodawer, A.,Waugh, D.S. (deposition date: 2002-05-28, release date: 2002-11-27, Last modification date: 2024-11-06)

Primary citation

Phan, J.,Zdanov, A.,Evdokimov, A.G.,Tropea, J.E.,Peters III, H.K.,Kapust, R.B.,Li, M.,Wlodawer, A.,Waugh, D.S.
Structural basis for the substrate specificity of tobacco etch virus protease.
J.Biol.Chem., 277:50564-50572, 2002

PubMed Abstract: 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.

PubMed: 12377789
DOI: 10.1074/jbc.M207224200

Experimental method

X-RAY DIFFRACTION (2.2 Å)