Crystal structure of amine oxidase from bovine serum.
Copper-containing amine oxidase extracted from bovine serum (BSAO) was crystallized and its three-dimensional structure at 2.37A resolution is described. The biological unit of BSAO is a homodimer, formed by two monomers related to each other by a non-crystallographic 2-fold axis. Each monomer is composed of three domains, similar to those of other amine oxidases from lower species. The two monomers are structurally equivalent, despite some minor differences at the two active sites. A large funnel allows access of substrates to the active-site; another cavity, accessible to the solvent, is also present between the two monomers; this second cavity could allow the entrance of molecular oxygen necessary for the oxidative reaction. Some sugar residues, bound to Asn, were still present and visible in the electron density map, in spite of the exhaustive deglycosylation necessary to grow the crystals. The comparison of the BSAO structure with those of other resolved AO structures shows strong dissimilarities in the architecture and charge distribution of the cavities leading to the active-site, possibly explaining the differences in substrate specificity.
Lunelli
Michele
M
Department of Biological Chemistry, University of Padua, Viale G. Colombo 3, 35121 Padua, Italy.
Di Paolo
Maria Luisa
ML
Biadene
Marianna
M
Calderone
Vito
V
Battistutta
Roberto
R
Scarpa
Marina
M
Rigo
Adelio
A
Zanotti
Giuseppe
G
D006631:Amine Oxidase (Copper-Containing) / Q000097:blood* / Q000737:chemistry*; D000818:Animals; D001665:Binding Sites; D002412:Cations / Q000378:metabolism; D002417:Cattle; D018360:Crystallography, X-Ray; D006031:Glycosylation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D044967:Serum / Q000737:chemistry*; D014978:Xenon / Q000378:metabolism
D002412:Cations; D021122:Protein Subunits; D014978:Xenon; D006631:Amine Oxidase (Copper-Containing)