3PGB

Crystal structure of Aspergillus nidulans amine oxidase

Summary for 3PGB

• Entry DOI: 10.2210/pdb3pgb/pdb
• Descriptor: Putative uncharacterized protein, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: oxidoreductase, copper amine oxidase, cao, topaquinone, tpq
• Biological source: Emericella nidulans (Aspergillus nidulans)
• Total number of polymer chains: 1
• Total formula weight: 92629.38

Authors

McGrath, A.P.,Guss, J.M. (deposition date: 2010-11-01, release date: 2011-07-13, Last modification date: 2023-11-01)

Primary citation

McGrath, A.P.,Mithieux, S.M.,Collyer, C.A.,Bakhuis, J.G.,van den Berg, M.,Sein, A.,Heinz, A.,Schmelzer, C.,Weiss, A.S.,Guss, J.M.
Structure and Activity of Aspergillus nidulans Copper Amine Oxidase
Biochemistry, 50:5718-5730, 2011

PubMed Abstract: Aspergillus nidulans amine oxidase (ANAO) has the unusual ability among the family of copper and trihydroxyphenylalanine quinone-containing amine oxidases of being able to oxidize the amine side chains of lysine residues in large peptides and proteins. We show here that in common with the related enzyme from the yeast Pichia pastoris, ANAO can promote the cross-linking of tropoelastin and oxidize the lysine residues in α-casein proteins and tropoelastin. The crystal structure of ANAO, the first for a fungal enzyme in this family, has been determined to a resolution of 2.4 Å. The enzyme is a dimer with the archetypal fold of a copper-containing amine oxidase. The active site is the most open of any of those of the structurally characterized enzymes in the family and provides a ready explanation for its lysine oxidase-like activity.

PubMed: 21604787
DOI: 10.1021/bi200555c

Experimental method

X-RAY DIFFRACTION (2.45 Å)