4EF3

Multicopper Oxidase CueO (Citrate buffer)

Summary for 4EF3

• Entry DOI: 10.2210/pdb4ef3/pdb
• Descriptor: Blue copper oxidase CueO, COPPER (II) ION, HYDROXIDE ION, ... (6 entities in total)
• Functional Keywords: multicopper oxidase, metal binding protein
• Biological source: Escherichia coli
• Cellular location: Periplasm: P36649
• Total number of polymer chains: 1
• Total formula weight: 54019.65

Authors

Komori, H.,Kataoka, K.,Sakurai, T.,Higuchi, Y. (deposition date: 2012-03-29, release date: 2013-05-22, Last modification date: 2024-03-20)

Primary citation

Komori, H.,Kataoka, K.,Tanaka, S.,Matsuda, N.,Higuchi, Y.,Sakurai, T.
Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity.
Acta Crystallogr.,Sect.F, 72:558-563, 2016

PubMed Abstract: The acetate-bound form of the type II copper was found in the X-ray structure of the multicopper oxidase CueO crystallized in acetate buffer in addition to the conventional OH(-)-bound form as the major resting form. The acetate ion was retained bound to the type II copper even after prolonged exposure of a CueO crystal to X-ray radiation, which led to the stepwise reduction of the Cu centres. However, in this study, when CueO was crystallized in citrate buffer the OH(-)-bound form was present exclusively. This fact shows that an exogenous acetate ion reaches the type II Cu centre through the water channel constructed between domains 1 and 3 in the CueO molecule. It was also found that the enzymatic activity of CueO is enhanced in the presence of acetate ions in the solvent water.

PubMed: 27380373
DOI: 10.1107/S2053230X16009237

Experimental method

X-RAY DIFFRACTION (1.9 Å)