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Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli
Published on: March 16, 2011
Function and molecular evolution of multicopper blue proteins
1Quantum Bioinformatics Group. Center for Promotion of Computational Science and Engineering, Japan Atomic Energy Research Institute, 801, Umemidai Soraku-gun, Kyoto 619-0215, Japan. kenske@apr.jaeri.go.jp
Abstract:
Multicopper blue proteins (MCBPs) are multidomain proteins that utilize the distinctive redox ability of copper ions. There are a variety of MCBPs that have been roughly classified into three different groups, based on their domain organization and functions: (i) nitrite reductase-type with two domains, (ii) laccase-type with three domains, and (iii) ceruloplasmin-type with six domains. Together, the second and third group are often commonly called multicopper oxidases (MCOs). The rapid accumulation of genome sequence information in recent years has revealed several new types of proteins containing MCBP domains, mainly from bacteria. In this review, the recent research on the functions and structures of MCBPs is summarized, mainly focusing on the new types. The latter half of this review focusses on the two domain MCBPs, which we propose as the evolutionary intermediate of the MCBP family.
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