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Crystal structures of E. coli laccase CueO at different copper concentrations.

Li X, Wei Z, Zhang M, Peng X, Yu G, Teng M, Gong W
Biochem Biophys Res Commun 354 21-6 (2007)
Related entries: 2fqd, 2fqe, 2fqg

Cited: 38 times
EuropePMC logo PMID: 17217912

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.

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  17. Structural and functional characterisation of multi-copper oxidase CueO from lignin-degrading bacterium Ochrobactrum sp. reveal its activity towards lignin model compounds and lignosulfonate. Granja-Travez RS, Wilkinson RC, Persinoti GF, Squina FM, Fülöp V, Bugg TDH. FEBS J 285 1684-1700 (2018)
  18. Molecular modeling and simulation studies of recombinant laccase from Yersinia enterocolitica suggests significant role in the biotransformation of non-steroidal anti-inflammatory drugs. Singh D, Rawat S, Waseem M, Gupta S, Lynn A, Nitin M, Ramchiary N, Sharma KK. Biochem Biophys Res Commun 469 306-312 (2016)
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  20. An enzymatic system for decolorization of wastewater dyes using immobilized CueO laccase-like multicopper oxidase on poly-3-hydroxybutyrate. Bello-Gil D, Roig-Molina E, Fonseca J, Sarmiento-Ferrández MD, Ferrándiz M, Franco E, Mira E, Maestro B, Sanz JM. Microb Biotechnol 11 881-892 (2018)
  21. Elucidation of the crystal structure of Coriolopsis caperata laccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions. Glazunova OA, Polyakov KM, Fedorova TV, Dorovatovskii PV, Koroleva OV. Acta Crystallogr D Biol Crystallogr 71 854-861 (2015)
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  28. Axial bonds at the T1 Cu site of Thermus thermophilus SG0.5JP17-16 laccase influence enzymatic properties. Zhu Y, Zhang Y, Zhan J, Lin Y, Yang X. FEBS Open Bio 9 986-995 (2019)
  29. Deep sequencing unveils altered cardiac miRNome in congenital heart disease. Ramachandran V, Bhagavatheeswaran S, Shanmugam S, Vasudevan M, Ragunathan M, Cherian KM, Munirajan AK, Ravi S, Balakrishnan A. Mol Genet Genomics 297 1123-1139 (2022)
  30. Gene cloning, identification, and characterization of the multicopper oxidase CumA from Pseudomonas sp. 593. Yang S, Long Y, Yan H, Cai H, Li Y, Wang X. Biotechnol Appl Biochem 64 347-355 (2017)
  31. A Novel Polyphenol Oxidoreductase OhLac from Ochrobactrum sp. J10 for Lignin Degradation. Yang C, Ma L, Wang X, Xing Y, Lü X. Front Microbiol 12 694166 (2021)
  32. A new multicopper oxidase from Gram-positive bacterium Rhodococcus erythropolis with activity modulating methionine rich tail. Classen T, Pietruszka J, Schuback SM. Protein Expr Purif 89 97-108 (2013)
  33. Crystal structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity. Wang H, Liu X, Zhao J, Yue Q, Yan Y, Gao Z, Dong Y, Zhang Z, Fan Y, Tian J, Wu N, Gong Y. Sci Rep 8 14252 (2018)
  34. Engineering Klebsiella sp. 601 multicopper oxidase enhances the catalytic efficiency towards phenolic substrates. Li Y, Gong Z, Li X, Li Y, Wang XG. BMC Biochem 12 30 (2011)
  35. Comparative analysis of Listeria monocytogenes plasmid transcriptomes reveals common and plasmid-specific gene expression patterns and high expression of noncoding RNAs. Anast JM, Etter AJ, Schmitz-Esser S. Microbiologyopen 11 e1315 (2022)
  36. Desulfovibrio DA2_CueO is a novel multicopper oxidase with cuprous, ferrous and phenol oxidase activity. Mancini S, Kumar R, Mishra V, Solioz M. Microbiology (Reading) 163 1229-1236 (2017)
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