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  • Title: Domain mobility as probed by small-angle X-ray scattering may account for substrate access to the active site of two copper-dependent amine oxidases.
    Author: Dainese E, Sabatucci A, Pintus F, Medda R, Angelucci CB, Floris G, Maccarrone M.
    Journal: Acta Crystallogr D Biol Crystallogr; 2014 Aug; 70(Pt 8):2101-10. PubMed ID: 25084330.
    Abstract:
    Amine oxidases are a family of dimeric enzymes that contain one copper(II) ion and one 2,4,5-trihydroxyphenyalanine quinone per subunit. Here, the low-resolution structures of two Cu/TPQ amine oxidases from lentil (Lens esculenta) seedlings and from Euphorbia characias latex have been determined in solution by small-angle X-ray scattering. The active site of these enzymes is highly buried and requires a conformational change to allow substrate access. The study suggests that the funnel-shaped cavity located between the D3 and D4 domains is narrower within the crystal structure, whereas in solution the D3 domain could undergo movement resulting in a protein conformational change that is likely to lead to easier substrate access.
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