Three-dimensional structure of laccase from Coriolus zonatus at 2.6 angstrom resolution

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

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

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 angstrom resolution (R (factor) = 21.23%, R (free) = 23.82%, rms deviations for the bond lengths and bond angles are 0.008 angstrom and 1.19 degrees, 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.

Original languageEnglish
Pages (from-to)817-823
Number of pages7
JournalCrystallography Reports
Volume51
DOIs
Publication statusPublished - Oct 2006

Keywords

  • CRYSTAL-STRUCTURE
  • COPRINUS-CINEREUS
  • SUBSTRATE
  • KINETICS
  • OXIDASE
  • MODEL

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