Three-dimensional structure of laccase from Coriolus zonatus at 2.6 Å resolution |
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| Authors: | A. V. Lyashenko Yu. N. Zhukova N. E. Zhukhlistova V. N. Zaitsev E. V. Stepanova G. S. Kachalova O. V. Koroleva W. Voelter Ch. Betzel V. I. Tishkov I. Bento A. G. Gabdulkhakov E. Yu. Morgunova P. F. Lindley A. M. Mikhailov |
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| Affiliation: | (1) Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskiĭ pr. 59, Moscow, 119333, Russia;(2) Centre for Biomolecular Sciences, University of St. Andrews, North Haugh, St. Andrews, Fife, KY16 9ST, UK;(3) Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskiĭ pr. 33, Moscow, 119991, Russia;(4) Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino Moscow oblast, 142290, Russia;(5) Institute for Biochemistry, University of Tübingen, Germany;(6) Department of Biochemistry and Molecular Biology, University of Hamburg, c/o DESY, Bld. 22a, Notkestrasse 85, D-22603 Hamburg, Germany;(7) Department of Chemical Enzymology, Moscow State University, Vorob’evy gory, Moscow, 119992, Russia;(8) Institute for Technology in Chemistry and Biology, New University of Lisbon, 127 Av. da Republica, 2781-901 Oeiras, Portugal;(9) Institute of Protein Research, Russian Academy of Sciences, Institutskaya ul. 4, Pushchino, Moscow oblast, 142290, Russia |
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| Abstract: | ![]()
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 Å resolution (R factor = 21.23%, R free = 23.82%, rms deviations for the bond lengths and bond angles are 0.008 Å 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. |
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