Structure and molecular evolution of multicopper blue proteins
The multicopper blue protein family, which contains cupredoxin-like domains as a structural unit, is one of the most diverse groups of proteins. This protein family is divided into two functionally different types of enzymes: multicopper oxidase and nitrite reductase. Multicopper oxidase catalyzes t...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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De Gruyter
2010-05-01
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| Series: | Biomolecular Concepts |
| Subjects: | |
| Online Access: | https://doi.org/10.1515/bmc.2010.004 |
| _version_ | 1819019136812974080 |
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| author | Komori Hirofumi Higuchi Yoshiki |
| author_facet | Komori Hirofumi Higuchi Yoshiki |
| author_sort | Komori Hirofumi |
| collection | DOAJ |
| description | The multicopper blue protein family, which contains cupredoxin-like domains as a structural unit, is one of the most diverse groups of proteins. This protein family is divided into two functionally different types of enzymes: multicopper oxidase and nitrite reductase. Multicopper oxidase catalyzes the oxidation of the substrate and then reduces dioxygen. The structures of many multicopper oxidases are already known, and until recently they were classified into two main groups: the three- and six-domain types. Both function as monomers and have three spectroscopically different copper sites: Types I (blue), II, and III (tri-nuclear). Nitrite reductase is a closely related protein that contains Types I and II (mono-nuclear) coppers but reduces nitrite instead of dioxygen. Nitrite reductase, which consists of two domains, forms a homotrimer. Multicopper oxidase and nitrite reductase share similar structural architectures and also contain Type I copper. Therefore, it is proposed that they have a common ancestor protein. Recently, some two-domain type multicopper oxidases have been found and their crystal structures have been determined. They have a trimeric quaternary structure and contain an active site at the molecular interface such as nitrite reductase. These results support previous hypotheses and provide an insight into the molecular evolution of multicopper blue proteins. |
| first_indexed | 2024-12-21T03:30:31Z |
| format | Article |
| id | doaj.art-9eaaa3b4258a4e2ba01c9833ed11d432 |
| institution | Directory Open Access Journal |
| issn | 1868-5021 1868-503X |
| language | English |
| last_indexed | 2024-12-21T03:30:31Z |
| publishDate | 2010-05-01 |
| publisher | De Gruyter |
| record_format | Article |
| series | Biomolecular Concepts |
| spelling | doaj.art-9eaaa3b4258a4e2ba01c9833ed11d4322022-12-21T19:17:28ZengDe GruyterBiomolecular Concepts1868-50211868-503X2010-05-0111314010.1515/bmc.2010.004Structure and molecular evolution of multicopper blue proteinsKomori HirofumiHiguchi YoshikiThe multicopper blue protein family, which contains cupredoxin-like domains as a structural unit, is one of the most diverse groups of proteins. This protein family is divided into two functionally different types of enzymes: multicopper oxidase and nitrite reductase. Multicopper oxidase catalyzes the oxidation of the substrate and then reduces dioxygen. The structures of many multicopper oxidases are already known, and until recently they were classified into two main groups: the three- and six-domain types. Both function as monomers and have three spectroscopically different copper sites: Types I (blue), II, and III (tri-nuclear). Nitrite reductase is a closely related protein that contains Types I and II (mono-nuclear) coppers but reduces nitrite instead of dioxygen. Nitrite reductase, which consists of two domains, forms a homotrimer. Multicopper oxidase and nitrite reductase share similar structural architectures and also contain Type I copper. Therefore, it is proposed that they have a common ancestor protein. Recently, some two-domain type multicopper oxidases have been found and their crystal structures have been determined. They have a trimeric quaternary structure and contain an active site at the molecular interface such as nitrite reductase. These results support previous hypotheses and provide an insight into the molecular evolution of multicopper blue proteins.https://doi.org/10.1515/bmc.2010.004ascorbate reductaseblue copperceruloplasminlaccasemulticopper oxidasenitrite reductasetype i copper |
| spellingShingle | Komori Hirofumi Higuchi Yoshiki Structure and molecular evolution of multicopper blue proteins Biomolecular Concepts ascorbate reductase blue copper ceruloplasmin laccase multicopper oxidase nitrite reductase type i copper |
| title | Structure and molecular evolution of multicopper blue proteins |
| title_full | Structure and molecular evolution of multicopper blue proteins |
| title_fullStr | Structure and molecular evolution of multicopper blue proteins |
| title_full_unstemmed | Structure and molecular evolution of multicopper blue proteins |
| title_short | Structure and molecular evolution of multicopper blue proteins |
| title_sort | structure and molecular evolution of multicopper blue proteins |
| topic | ascorbate reductase blue copper ceruloplasmin laccase multicopper oxidase nitrite reductase type i copper |
| url | https://doi.org/10.1515/bmc.2010.004 |
| work_keys_str_mv | AT komorihirofumi structureandmolecularevolutionofmulticopperblueproteins AT higuchiyoshiki structureandmolecularevolutionofmulticopperblueproteins |