A C-terminal disulfide bond in the copper-containing amine oxidase from pea seedlings violates the twofold symmetry of the molecular dimer.

ABSTRACT: The structure of a newly crystallized form of the copper-dependent amine oxidase from pea seedlings has been refined at a resolution of 2.2 A to a final R factor of 0.181. The structure (form II) was originally discovered during a study of xenon binding to copper-dependent amine oxidases as a probe for dioxygen-binding sites [Duff et al. (2004), J. Mol. Biol. 344, 599-607]. The form II crystals belong to space group P2(1), with two dimers in the asymmetric unit. The overall structure is very similar to the crystals of form I in space group P2(1)2(1)2(1) with a dimer in the asymmetric unit [Kumar et al. (1996), Structure, 4, 943-955]. In form I the last three residues (644-647) observable in the two subunits were apparently splayed apart. It was noted that the absence of a disulfide bond be

SUBMITTER: Duff AP 

PROVIDER: S-EPMC2225380 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature