2FQE

Crystal Structures of E. coli Laccase CueO under different copper binding situations

Summary for 2FQE

• Entry DOI: 10.2210/pdb2fqe/pdb
• Related: 2FQD 2FQF 2FQG
• Descriptor: Blue copper oxidase cueO, COPPER (II) ION, SODIUM ION, ... (6 entities in total)
• Functional Keywords: azurin-like domain, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P36649
• Total number of polymer chains: 1
• Total formula weight: 53968.58

Authors

Li, X.,Wei, Z.,Zhang, M.,Teng, M.,Gong, W. (deposition date: 2006-01-18, release date: 2007-01-30, Last modification date: 2024-03-13)

Primary citation

Li, X.,Wei, Z.,Zhang, M.,Peng, X.,Yu, G.,Teng, M.,Gong, W.
Crystal structures of E. coli laccase CueO at different copper concentrations.
Biochem.Biophys.Res.Commun., 354:21-26, 2007

PubMed Abstract: CueO protein is a hypothetical bacterial laccase and a good laccase candidate for large scale industrial application. Four CueO crystal structures were determined at different copper concentrations. Low copper occupancy in apo-CueO and slow copper reconstitution process in CueO with exogenous copper were demonstrated. These observations well explain the copper dependence of CueO oxidase activity. Structural comparison between CueO and other three fungal laccase proteins indicates that Glu106 in CueO constitutes the primary counter-work for reconstitution of the trinuclear copper site. Mutation of Glu106 to a Phe enhanced CueO oxidation activity and supported this hypothesis. In addition, an extra alpha-helix from Leu351 to Gly378 covers substrate biding pocket of CueO and might compromises the electron transfer from substrate to type I copper.

PubMed: 17217912
DOI: 10.1016/j.bbrc.2006.12.116

Experimental method

X-RAY DIFFRACTION (1.92 Å)