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

doi:10.1134/S1063774506050117

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

School of Chemistry

Research output: Contribution to journal › Article › peer-review

15 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 language	English
Pages (from-to)	817-823
Number of pages	7
Journal	Crystallography Reports
Volume	51
DOIs	https://doi.org/10.1134/S1063774506050117
Publication status	Published - Oct 2006

Keywords

CRYSTAL-STRUCTURE
COPRINUS-CINEREUS
SUBSTRATE
KINETICS
OXIDASE
MODEL

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10.1134/S1063774506050117

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Lyashenko, A. V., Zhukova, Y. N., Zhukhlistova, N. E., Zaitsev, V. N., Stepanova, E. V., Kachalova, G. S., Koroleva, O. V., Voelter, W., Betzel, C., Tishkov, V. I., Bento, I., Gabdulkhakov, A. G., Morgunova, E. Y., Lindley, P. F., & Mikhailov, A. M. (2006). Three-dimensional structure of laccase from Coriolus zonatus at 2.6 angstrom resolution. Crystallography Reports, 51, 817-823. https://doi.org/10.1134/S1063774506050117

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title = "Three-dimensional structure of laccase from Coriolus zonatus at 2.6 angstrom resolution",

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.",

keywords = "CRYSTAL-STRUCTURE, COPRINUS-CINEREUS, SUBSTRATE, KINETICS, OXIDASE, MODEL",

author = "Lyashenko, {A. V.} and Zhukova, {Yu. N.} and Zhukhlistova, {N. E.} and Zaitsev, {V. N.} and Stepanova, {E. V.} and Kachalova, {G. S.} and Koroleva, {O. V.} and W. Voelter and Ch. Betzel and Tishkov, {V. I.} and I. Bento and Gabdulkhakov, {A. G.} and Morgunova, {E. Yu.} and Lindley, {P. F.} and Mikhailov, {A. M.}",

year = "2006",

month = oct,

doi = "10.1134/S1063774506050117",

language = "English",

volume = "51",

pages = "817--823",

journal = "Crystallography Reports",

issn = "1562-689X",

publisher = "Maik Nauka-Interperiodica Publishing",

}

Lyashenko, AV, Zhukova, YN, Zhukhlistova, NE, Zaitsev, VN, Stepanova, EV, Kachalova, GS, Koroleva, OV, Voelter, W, Betzel, C, Tishkov, VI, Bento, I, Gabdulkhakov, AG, Morgunova, EY, Lindley, PF & Mikhailov, AM 2006, 'Three-dimensional structure of laccase from Coriolus zonatus at 2.6 angstrom resolution', Crystallography Reports, vol. 51, pp. 817-823. https://doi.org/10.1134/S1063774506050117

TY - JOUR

T1 - Three-dimensional structure of laccase from Coriolus zonatus at 2.6 angstrom resolution

AU - Lyashenko, A. V.

AU - Zhukova, Yu. N.

AU - Zhukhlistova, N. E.

AU - Zaitsev, V. N.

AU - Stepanova, E. V.

AU - Kachalova, G. S.

AU - Koroleva, O. V.

AU - Voelter, W.

AU - Betzel, Ch.

AU - Tishkov, V. I.

AU - Bento, I.

AU - Gabdulkhakov, A. G.

AU - Morgunova, E. Yu.

AU - Lindley, P. F.

AU - Mikhailov, A. M.

PY - 2006/10

Y1 - 2006/10

N2 - 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.

AB - 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.

KW - CRYSTAL-STRUCTURE

KW - COPRINUS-CINEREUS

KW - SUBSTRATE

KW - KINETICS

KW - OXIDASE

KW - MODEL

UR - http://www.scopus.com/inward/record.url?scp=33749258360&partnerID=8YFLogxK

U2 - 10.1134/S1063774506050117

DO - 10.1134/S1063774506050117

M3 - Article

SN - 1562-689X

VL - 51

SP - 817

EP - 823

JO - Crystallography Reports

JF - Crystallography Reports

ER -

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

Abstract

Keywords

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