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. (1st August 2014)

• Record Type: Journal Article
• Authors: Dainese, Enrico; Sabatucci, Annalaura; Pintus, Francesca; Medda, Rosaria; Angelucci, Clotilde Beatrice; Floris, Giovanni; Maccarrone, Mauro
• Is Part Of: Acta crystallographica. Volume 70:Part 8(2014:Aug.)
• Page Start: 2101
• Page End: 2110
• Publication Date: 2014-08-01
• Subjects: Biomolecules -- Structure -- Periodicals; Physical biochemistry -- Periodicals; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; 572
• DOI: 10.1107/S1399004714012140
• Languages: English
• ISSNs: 0907-4449

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 (<italic>Lens esculenta</italic>) seedlings and from <italic>Euphorbia characias</italic> 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.</p> </abstract>