1Q31
Crystal Structure of the Tobacco Etch Virus Protease C151A mutant
Summary for 1Q31
| Entry DOI | 10.2210/pdb1q31/pdb |
| Related | 1LVB 1LVM |
| Descriptor | Nuclear inclusion protein A, BETA-MERCAPTOETHANOL (3 entities in total) |
| Functional Keywords | 3c-type protease, tev, two-domain, antiparallel, beta-barrel, trypsin-like, c151a, viral protein, hydrolase |
| Biological source | Tobacco etch virus |
| Cellular location | Capsid protein: Virion (Potential): P04517 |
| Total number of polymer chains | 2 |
| Total formula weight | 55210.60 |
| Authors | Nunn, C.M.,Djordjevic, S.,George, R.R.,Urquhart, G.T.,Chao, L.H.,Tsuchiya, Y. (deposition date: 2003-07-28, release date: 2004-11-02, Last modification date: 2023-10-25) |
| Primary citation | Nunn, C.M.,Jeeves, M.,Cliff, M.J.,Urquhart, G.T.,George, R.R.,Chao, L.H.,Tscuchia, Y.,Djordjevic, S. Crystal structure of tobacco etch virus protease shows the protein C terminus bound within the active site. J.Mol.Biol., 350:145-155, 2005 Cited by PubMed 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 2.7A 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. PubMed: 15919091DOI: 10.1016/j.jmb.2005.04.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report
