3wa2

High resolution crystal structure of copper amine oxidase from arthrobacter globiformis

spinqualitylabelsall models 3wa2, resolution 1.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wa2 is a 1 chain structure with sequence from Arthrobacter globiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.08Å Ligands: 1PE, CU, EDO, NA, OXY, PEG, PG4, PGE, TPQ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAOX_ARTGO Publication Abstract from PubMed The crystal structure of a copper amine oxidase from Arthrobacter globiformis was determined at 1.08 A resolution with the use of low-molecular-weight polyethylene glycol (LMW PEG; average molecular weight approximately 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 approximately 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. High-resolution crystal structure of copper amine oxidase from Arthrobacter globiformis: assignment of bound diatomic molecules as O2.,Murakawa T, Hayashi H, Sunami T, Kurihara K, Tamada T, Kuroki R, Suzuki M, Tanizawa K, Okajima T Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2483-94. doi:, 10.1107/S0907444913023196. Epub 2013 Nov 19. PMID:24311589 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Copper amine oxidase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA