1D6U

CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE

Summary for 1D6U

• Entry DOI: 10.2210/pdb1d6u/pdb
• Related: 1D6U 1D6Y 1D6Z 1JEZ 1OAC 1QAF 1QAK 1QAL 1SPU
• Descriptor: COPPER AMINE OXIDASE, COPPER (II) ION, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: reaction intermediate, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P46883
• Total number of polymer chains: 2
• Total formula weight: 163569.59

Authors

Wilmot, C.M.,Hajdu, J.,McPherson, M.J.,Knowles, P.F.,Phillips, S.E.V. (deposition date: 1999-10-15, release date: 2000-02-02, Last modification date: 2024-03-13)

Primary citation

Wilmot, C.M.,Hajdu, J.,McPherson, M.J.,Knowles, P.F.,Phillips, S.E.
Visualization of dioxygen bound to copper during enzyme catalysis.
Science, 286:1724-1728, 1999

PubMed Abstract: X-ray crystal structures of three species related to the oxidative half of the reaction of the copper-containing quinoprotein amine oxidase from Escherichia coli have been determined. Crystals were freeze-trapped either anaerobically or aerobically after exposure to substrate, and structures were determined to resolutions between 2.1 and 2.4 angstroms. The oxidation state of the quinone cofactor was investigated by single-crystal spectrophotometry. The structures reveal the site of bound dioxygen and the proton transfer pathways involved in oxygen reduction. The quinone cofactor is regenerated from the iminoquinone intermediate by hydrolysis involving Asp383, the catalytic base in the reductive half-reaction. Product aldehyde inhibits the hydrolysis, making release of product the rate-determining step of the reaction in the crystal.

PubMed: 10576737
DOI: 10.1126/science.286.5445.1724

Experimental method

X-RAY DIFFRACTION (2.4 Å)