1Q31

Crystal Structure of the Tobacco Etch Virus Protease C151A mutant

1Q31 の概要

• エントリーDOI: 10.2210/pdb1q31/pdb
• 関連するPDBエントリー: 1LVB 1LVM
• 分子名称: Nuclear inclusion protein A, BETA-MERCAPTOETHANOL (3 entities in total)
• 機能のキーワード: 3c-type protease, tev, two-domain, antiparallel, beta-barrel, trypsin-like, c151a, viral protein, hydrolase
• 由来する生物種: Tobacco etch virus
• 細胞内の位置: Capsid protein: Virion (Potential): P04517
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55210.60

構造登録者

Nunn, C.M.,Djordjevic, S.,George, R.R.,Urquhart, G.T.,Chao, L.H.,Tsuchiya, Y. (登録日: 2003-07-28, 公開日: 2004-11-02, 最終更新日: 2023-10-25)

主引用文献

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

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: 15919091
DOI: 10.1016/j.jmb.2005.04.013

実験手法

X-RAY DIFFRACTION (2.7 Å)