page_title: TEV protease
section_title: Structure and function
hierarchical_section_title: TEV protease / Structure and function
caption_attribution_description: English: Structure of TEV protease. The double β-barrels that define the superfamily are highlighted in red. The final 15 amino acids (222-236) of the enzyme C-terminus are not visible in the structure as they are too flexible (PDB 1lvb)
context_page_description: TEV protease is a highly sequence-specific cysteine protease from Tobacco Etch Virus. It is a member of the PA clan of chymotrypsin-like proteases. Due to its high sequence specificity it is frequently used for the controlled cleavage of fusion proteins in vitro and in vivo.
context_section_description: The structure of TEV protease has been solved by X-ray crystallography. It is composed of two β-barrels and a flexible C-terminal tail and displays structural homology to the chymotrypsin superfamily of proteases (PA clan, C4 family by MEROPS classification). Although homologous to cellular serine proteases (such as trypsin, elastase, thrombin etc.), TEV protease uses a cysteine as its catalytic nucleophile (as do many other viral proteases).
  Covalent catalysis is performed with an Asp-His-Cys triad, split between the two barrels (Asp on β1 and His and Cys on β2). The substrate is held as a β-sheet, forming an antiparallel interaction with the cleft between the barrels and a parallel interaction with the C-terminal tail. The enzyme therefore forms a binding tunnel around the substrate and side chain interactions control specificity.
caption: Structure of TEV protease. The double β-barrels that define the superfamily are highlighted in red. (PDB: 1lvm​)
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