Three-dimensional structure of laccase from Coriolus zonatus at 2.6 Å resolution
| Autor: | Azat Gabdulkhakov, Al'bert M. Mikhailov, A. V. Lyashenko, Elena V. Stepanova, I. Bento, Vladimir I. Tishkov, Yu. N. Zhukova, N. E. Zhukhlistova, Ch. Betzel, P. F. Lindley, E. Yu. Morgunova, O. V. Koroleva, Wolfang Voelter, Galina S. Kachalova, Viatcheslav Zaitsev |
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| Rok vydání: | 2006 |
| Předmět: |
chemistry.chemical_classification
Laccase biology Stereochemistry Inorganic chemistry Active site chemistry.chemical_element General Chemistry Condensed Matter Physics Oxygen Bond length chemistry.chemical_compound Molecular geometry chemistry Oxidoreductase biology.protein Molecule General Materials Science Hydrogen peroxide |
| Zdroj: | Crystallography Reports. 51:817-823 |
| ISSN: | 1562-689X 1063-7745 |
| Popis: | Laccase (oxygen oxidoreductase, EC 1.14.18.1) belongs to the copper-containing oxidases. This enzyme catalyzes reduction of molecular oxygen by different organic and inorganic compounds to water without the formation of hydrogen peroxide. The three-dimensional structure of native laccase from Coriolus zonatus was solved and refined at 2.6 A resolution (Rfactor = 21.23%, Rfree = 23.82%, rms deviations for the bond lengths and bond angles are 0.008 A and 1.19°, respectively). The primary structure of the polypeptide chain and the architecture of the active site were refined. The carbohydrate component of the enzyme was identified. The access and exit water channels providing the access of molecular oxygen to the active site and release of water, which is the reduction product of molecular oxygen, from the protein molecule were found in the structure. |
| Databáze: | OpenAIRE |
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