1q31: Difference between revisions

[[Image:1q31.gif|left|200px]]<br /><applet load="1q31" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

1Q31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tobacco_etch_virus Tobacco etch virus] with <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q31 OCA].  

[[Category: Chao, L H.]]

[[Category: George, R R.]]

[[Category: Nunn, C M.]]

[[Category: Urquhart, G T.]]

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