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Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting

  1. Author:
    Kervinen, J.
    Tobin, G. J.
    Costa, J.
    Waugh, D. S.
    Wlodawer, A.
    Zdanov, A.

  2. Author Address

    Zdanov A NCI, Prot Struct Sect, Frederick Canc Res & Dev Ctr Frederick, MD 21702 USA NCI, Prot Struct Sect, Frederick Canc Res & Dev Ctr Frederick, MD 21702 USA NCI, Prot Engn Grp,Macromol Struct Lab, ABL Basic Res Program, Frederick Canc Res & Dev Ctr Frederick, MD 21702 USA NCI, Lab Cell & Mol Struct SAIC, Frederick Canc Res & Dev Ctr Frederick, MD 21702 USA Univ Nova Lisboa, Inst Tecnol Quim & Biol, Inst Biol Expt & Tecnol P-2780 Oeiras Portugal
    1. Year: 1999
  2. Journal: Embo Journal
    1. 18
    2. 14
    3. Pages: 3947-3955
  4. Type of Article: Article
  1. Abstract:

    We determined at 2.3 Angstrom resolution the crystal structure of prophytepsin, a zymogen of a barley vacuolar aspartic proteinase. In addition to the classical pepsin-like bilobal main body of phytepsin, we also traced most of the propeptide, as well as an independent plant-specific domain, never before described in structural terms. The structure revealed that, in addition to the propeptide, 13 N-terminal residues of the mature phytepsin are essential for inactivation of the enzyme. Comparison of the plant-specific domain with NK-lysin indicates that these two saposin-like structures are closely related, suggesting that all saposins and saposin-like domains share a common topology. Structural analysis of prophytepsin led to the identification of a putative membrane receptor-binding site involved in Golgi-mediated transport to vacuoles. [References: 51]

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