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Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes

  1. Author:
    Wlodawer, A.
    Li, M.
    Dauter, Z.
    Gustchina, A.
    Uchida, K.
    Oyama, H.
    Dunn, B. M.
    Oda, K.

  2. Author Address

    NCI, Prot Struct Sect, Macromol Crystallog Lab, Frederick, MD 21702 USA. NCI, Prot Struct Sect, Macromol Crystallog Lab, Frederick, MD 21702 USA. NCI, Intramural Res Support Program, SAIC Frederick, Frederick, MD 21702 USA. Brookhaven Natl Lab, Natl Canc Inst, Macromol Crystallog Lab, Synchrotron Radiat Res Sect, Upton, NY 11973 USA. Brookhaven Natl Lab, NSLS, Upton, NY 11973 USA. Teikyo Univ, Sch Sci & Engn, Dept Biosci, Utsunomiya, Tochigi 3208551, Japan. Kyoto Inst Technol, Fac Text Sci, Dept Appl Biol, Sakyo Ku, Kyoto 6068585, Japan. Univ Florida, Dept Biochem & Mol Biol, Gainesville, FL 32610 USA. Wlodawer A NCI, Prot Struct Sect, Macromol Crystallog Lab, Frederick, MD 21702 USA.
    1. Year: 2001
  2. Journal: Nature Structural Biology
    1. 8
    2. 5
    3. Pages: 442-446
  4. Type of Article: Article
  1. Abstract:

    The crystal structure of a pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. 101 (PSCP) has been solved by single-wavelength anomalous diffraction using the absorption peak of bromide anions. Structures of the uninhibited enzyme and of complexes with an inhibitor that was either covalently or noncovalently bound were refined at 1.0-1.4 Angstrom resolution. The structure of PSCP comprises a single compact domain with a diameter of similar to 55 Angstrom, consisting of a seven-stranded parallel beta -sheet flanked on both sides by a number of helices. The fold of PSCP is a superset of the subtilisin fold, and the covalently bound inhibitor is linked to the enzyme through a serine residue. Thus, the structure of PSCP defines a novel family of serine-carboxyl proteinases (defined as MEROPS S53) with a unique catalytic triad consisting of Glu 80, Asp 84 and Ser 287.

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