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

Enrico Dainese, Annalaura Sabatucci, Francesca Pintus, Rosaria Medda, Clotilde Beatrice Angelucci, Giovanni Floris, Mauro Maccarrone

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)2101-2110
Number of pages10
JournalActa Crystallographica Section D: Biological Crystallography
Volume70
Issue number8
DOIs
Publication statusPublished - 2014

Keywords

  • amine oxidase
  • conformational change
  • copper
  • domain movement
  • SAXS
  • TOPA
  • TPQ

ASJC Scopus subject areas

  • Structural Biology
  • Medicine(all)

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