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Crystallization of cyclase-associated protein from Dictyostelium discoideum

  1. Author:
    Hofmann, A.
    Hess, S.
    Noegel, A. A.
    Schleicher, M.
    Wlodawer, A.

  2. Author Address

    NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA Univ Edinburgh, Inst Cell & Mol Biol, Edinburgh EH9 3JR, Midlothian, Scotland NIDDK, Struct Mass Spectrometry Facil, Bioorgan Chem Lab, NIH, Bethesda, MD 20892 USA Univ Cologne, Fak Med, Inst Biochem 1, D-5000 Cologne 41, Germany Univ Munich, Adolf Butenandt Inst, D-80336 Munich, Germany Hofmann A NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA
    1. Year: 2002
  2. Journal: Acta Crystallographica Section D-Biological Crystallography
    1. 58
    2. Part 10, Sp. Iss. 2
    3. Pages: 1858-1861
  4. Type of Article: Article
  1. Abstract:

    Cyclase-associated protein (CAP) is a conserved two-domain protein that helps to activate the catalytic activity of adenylyl cyclase in the cyclase-bound state through interaction with Ras, which binds to the cyclase in a different region. With its other domain, CAP can bind monomeric actin and therefore also carries a cytoskeletal function. The protein is thus involved in Ras/cAMP-dependent signal transduction and most likely serves as an adapter protein translocating the adenylyl cyclase complex to the actin cytoskeleton. Crystals belonging to the orthorhombic space group C222, with unit-cell parameters a = 71.2, b = 75.1, c = 162.9 Angstrom, have been obtained from Dictyostelium discoideum CAP carrying a C- terminal His tag. A complete native data set extending to 2.2 Angstrom resolution was collected from a single crystal using an in-house X-ray system. The asymmetric unit contains one molecule of CAP.

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