Summary for 4NER
| Entry DOI | 10.2210/pdb4ner/pdb |
| Related | 4E9Q 4E9R 4E9S 4E9T |
| Descriptor | Blue copper oxidase CueO, COPPER (II) ION, HYDROXIDE ION, ... (5 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 53827.53 |
| Authors | Komori, H.,Kataoka, K.,Sakurai, T.,Higuchi, Y. (deposition date: 2013-10-30, release date: 2014-03-12, Last modification date: 2024-03-20) |
| Primary citation | Komori, H.,Sugiyama, R.,Kataoka, K.,Miyazaki, K.,Higuchi, Y.,Sakurai, T. New insights into the catalytic active-site structure of multicopper oxidases. Acta Crystallogr.,Sect.D, 70:772-779, 2014 Cited by PubMed Abstract: Structural models determined by X-ray crystallography play a central role in understanding the catalytic mechanism of enzymes. However, X-ray radiation generates hydrated electrons that can cause significant damage to the active sites of metalloenzymes. In the present study, crystal structures of the multicopper oxidases (MCOs) CueO from Escherichia coli and laccase from a metagenome were determined. Diffraction data were obtained from a single crystal under low to high X-ray dose conditions. At low levels of X-ray exposure, unambiguous electron density for an O atom was observed inside the trinuclear copper centre (TNC) in both MCOs. The gradual reduction of copper by hydrated electrons monitored by measurement of the Cu K-edge X-ray absorption spectra led to the disappearance of the electron density for the O atom. In addition, the size of the copper triangle was enlarged by a two-step shift in the location of the type III coppers owing to reduction. Further, binding of O2 to the TNC after its full reduction was observed in the case of the laccase. Based on these novel structural findings, the diverse resting structures of the MCOs and their four-electron O2-reduction process are discussed. PubMed: 24598746DOI: 10.1107/S1399004713033051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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