title: A new crystal form of human diamine oxidase.
abstract: Copper amine oxidases (CAOs) are ubiquitous in nature and catalyse the oxidative deamination of primary amines to the corresponding aldehydes. Humans have three viable CAO genes (AOC1-3). AOC1 encodes human diamine oxidase (hDAO), which is the frontline enzyme for histamine metabolism. hDAO is unique among CAOs in that it has a distinct substrate preference for diamines. The structure of hDAO in space group P2(1)2(1)2(1) with two molecules in the asymmetric unit has recently been reported. Here, the structure of hDAO refined to 2.1 A resolution in space group C222(1) with one molecule in the asymmetric unit is reported.
authors.affiliation: School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia. a.mcgrath@mmb.usyd.edu.au
authors.forename: Aaron P
authors.initials: AP
authors.lastname: McGrath
authors.forename: Kimberly M
authors.initials: KM
authors.lastname: Hilmer
authors.forename: Charles A
authors.initials: CA
authors.lastname: Collyer
authors.forename: David M
authors.initials: DM
authors.lastname: Dooley
authors.forename: J Mitchell
authors.initials: JM
authors.lastname: Guss
mesh_terms: D006631:Amine Oxidase (Copper-Containing) / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D020134:Catalytic Domain; D002460:Cell Line; D018360:Crystallography, X-Ray; D004331:Drosophila melanogaster; D006801:Humans; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein
chemical_list: D006631:Amine Oxidase (Copper-Containing)