Acta Crystallographica Section D

Biological Crystallography

Volume 69, Part 12 (December 2013)


research papers



Acta Cryst. (2013). D69, 2483-2494    [ doi:10.1107/S0907444913023196 ]

High-resolution crystal structure of copper amine oxidase from Arthrobacter globiformis: assignment of bound diatomic molecules as O2

T. Murakawa, H. Hayashi, T. Sunami, K. Kurihara, T. Tamada, R. Kuroki, M. Suzuki, K. Tanizawa and T. Okajima

Abstract: The crystal structure of a copper amine oxidase from Arthrobacter globiformis was determined at 1.08 Å resolution with the use of low-molecular-weight polyethylene glycol (LMW PEG; average molecular weight ~200) as a cryoprotectant. The final crystallographic R factor and Rfree were 13.0 and 15.0%, respectively. Several molecules of LMW PEG were found to occupy cavities in the protein interior, including the active site, which resulted in a marked reduction in the overall B factor and consequently led to a subatomic resolution structure for a relatively large protein with a monomer molecular weight of ~70 000. About 40% of the presumed H atoms were observed as clear electron densities in the Fo - Fc difference map. Multiple minor conformers were also identified for many residues. Anisotropic displacement fluctuations were evaluated in the active site, which contains a post-translationally derived quinone cofactor and a Cu atom. Furthermore, diatomic molecules, most likely to be molecular oxygen, are bound to the protein, one of which is located in a region that had previously been proposed as an entry route for the dioxygen substrate from the central cavity of the dimer interface to the active site.

PDB references: 3wa2 and 3wa3

Keywords: copper amine oxidase; TPQ.


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[ doi:10.1107/S0907444913023196/tz5037sup1.pdf ]
Supplementary methods, figures and table.


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