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Tobacco etch virus protease: Crystal structure of the active enzyme and its inactive mutant

  1. Author:
    Zdanov, A. S.
    Phan, J.
    Evdokimov, A. G.
    Tropea, J. E.
    Peters, H. K.
    Kapust, R. B.
    Li, M.
    Wlodawer, A.
    Waugh, A. S.

  2. Author Address

    NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21702 USA NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21702 USA Zdanov AS NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21702 USA
    1. Year: 2003
  2. Journal: Russian Journal of Bioorganic Chemistry
    1. 29
    2. 5
    3. Pages: 415-417
  4. Type of Article: Article
  1. Abstract:

    Tobacco Etch Virus Protease (TEV protease) is widely used as a tool for separation of recombinant target proteins from their fusion partners. The crystal structures of two mutants of TEV protease, the active autolysis-resistant mutant TEV-S219D in complex with the proteolysis product, and the inactive mutant TEV-C151A in complex with a substrate, have been determined at 1.8 and 2.2 Angstrom resolution, respectively. The active sites of both mutants, including their oxyanion holes, have identical structures. The C-terminal residues 217-221 of the enzyme are involved in formation of the binding pockets S-3-S-6. This indicates that the autolysis of the peptide bond Met218-Ser219 exerts a strong effect on the fine-tuning of the substrate in the enzyme active site, which results in a considerable decrease n the enzymatic activity.

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