1q31
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Nuclear-inclusion-a_endopeptidase Nuclear-inclusion-a endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.44 3.4.22.44] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nuclear-inclusion-a_endopeptidase Nuclear-inclusion-a endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.44 3.4.22.44] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1lvb|1LVB]], [[1lvm|1LVM]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q31 OCA], [http://www.ebi.ac.uk/pdbsum/1q31 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q31 RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Tsuchiya, Y.]] | [[Category: Tsuchiya, Y.]] | ||
[[Category: Urquhart, G T.]] | [[Category: Urquhart, G T.]] | ||
| - | [[Category: BME]] | ||
[[Category: 3c-type protease]] | [[Category: 3c-type protease]] | ||
[[Category: antiparallel]] | [[Category: antiparallel]] | ||
| Line 38: | Line 40: | ||
[[Category: two-domain]] | [[Category: two-domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:08:09 2008'' |
Revision as of 20:08, 30 March 2008
| |||||||
| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Nuclear-inclusion-a endopeptidase, with EC number 3.4.22.44 | ||||||
| Related: | 1LVB, 1LVM
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Tobacco Etch Virus Protease C151A mutant
Overview
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.
About this Structure
1Q31 is a Single protein structure of sequence from Tobacco etch virus. Full crystallographic information is available from OCA.
Reference
Crystal structure of tobacco etch virus protease shows the protein C terminus bound within the active site., Nunn CM, Jeeves M, Cliff MJ, Urquhart GT, George RR, Chao LH, Tscuchia Y, Djordjevic S, J Mol Biol. 2005 Jul 1;350(1):145-55. PMID:15919091
Page seeded by OCA on Sun Mar 30 23:08:09 2008
