Comparative analysis of spatial organization of laccases from Cerrena maxima and Coriolus zonatus

Yu. N. Zhukova; N. E. Zhukhlistova; A. V. Lyashenko; E. Yu. Morgunova; V. N. Zaitsev; A. M. Mikhailov

doi:10.1134/S1063774507050124

Comparative analysis of spatial organization of laccases from Cerrena maxima and Coriolus zonatus

Yu. N. Zhukova, N. E. Zhukhlistova, A. V. Lyashenko, E. Yu. Morgunova, V. N. Zaitsev, A. M. Mikhailov

School of Chemistry

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

1 Citation (Scopus)

Abstract

Laccase (oxygen oxidoreductase, EC 1.10.3.2) belongs to the multicopper oxidase family. The main function of this enzyme is to perform electron transfer from the oxidized substrate through the mononuclear copper-containing site T1 to the oxygen molecule bound to the site T3 in the trinuclear T2/T3 cluster. The structures of two new fungal laccases from C. maxima and C. zonatus were solved on the basis of synchrotron X-ray diffraction data. Both laccases show high structural homology with laccases from other sources. The role of the carbohydrate component of laccases in structure stabilization and formation of ordered protein crystals was demonstrated. In the structures of C. maxima and C. zonatus laccases, two water channels of functional importance were found and characterized. The structural results reported in the present study characterize one of the functional states of the enzyme fixed in the crystal structure.

Original language	English
Pages (from-to)	826-837
Number of pages	12
Journal	Crystallography Reports
Volume	52
DOIs	https://doi.org/10.1134/S1063774507050124
Publication status	Published - Sept 2007

Keywords

WHITE-ROT FUNGI
CRYSTAL-STRUCTURE
ANGSTROM RESOLUTION
COPRINUS-CINEREUS
ASCORBATE OXIDASE
ELECTRON-TRANSFER
FULL COMPLEMENT
NITRIC-OXIDE
LIGNIN
SUBSTRATE

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title = "Comparative analysis of spatial organization of laccases from Cerrena maxima and Coriolus zonatus",

abstract = "Laccase (oxygen oxidoreductase, EC 1.10.3.2) belongs to the multicopper oxidase family. The main function of this enzyme is to perform electron transfer from the oxidized substrate through the mononuclear copper-containing site T1 to the oxygen molecule bound to the site T3 in the trinuclear T2/T3 cluster. The structures of two new fungal laccases from C. maxima and C. zonatus were solved on the basis of synchrotron X-ray diffraction data. Both laccases show high structural homology with laccases from other sources. The role of the carbohydrate component of laccases in structure stabilization and formation of ordered protein crystals was demonstrated. In the structures of C. maxima and C. zonatus laccases, two water channels of functional importance were found and characterized. The structural results reported in the present study characterize one of the functional states of the enzyme fixed in the crystal structure.",

keywords = "WHITE-ROT FUNGI, CRYSTAL-STRUCTURE, ANGSTROM RESOLUTION, COPRINUS-CINEREUS, ASCORBATE OXIDASE, ELECTRON-TRANSFER, FULL COMPLEMENT, NITRIC-OXIDE, LIGNIN, SUBSTRATE",

author = "Zhukova, {Yu. N.} and Zhukhlistova, {N. E.} and Lyashenko, {A. V.} and Morgunova, {E. Yu.} and Zaitsev, {V. N.} and Mikhailov, {A. M.}",

year = "2007",

month = sep,

doi = "10.1134/S1063774507050124",

language = "English",

volume = "52",

pages = "826--837",

journal = "Crystallography Reports",

issn = "1562-689X",

publisher = "Maik Nauka-Interperiodica Publishing",

}

TY - JOUR

T1 - Comparative analysis of spatial organization of laccases from Cerrena maxima and Coriolus zonatus

AU - Zhukova, Yu. N.

AU - Zhukhlistova, N. E.

AU - Lyashenko, A. V.

AU - Morgunova, E. Yu.

AU - Zaitsev, V. N.

AU - Mikhailov, A. M.

PY - 2007/9

Y1 - 2007/9

N2 - Laccase (oxygen oxidoreductase, EC 1.10.3.2) belongs to the multicopper oxidase family. The main function of this enzyme is to perform electron transfer from the oxidized substrate through the mononuclear copper-containing site T1 to the oxygen molecule bound to the site T3 in the trinuclear T2/T3 cluster. The structures of two new fungal laccases from C. maxima and C. zonatus were solved on the basis of synchrotron X-ray diffraction data. Both laccases show high structural homology with laccases from other sources. The role of the carbohydrate component of laccases in structure stabilization and formation of ordered protein crystals was demonstrated. In the structures of C. maxima and C. zonatus laccases, two water channels of functional importance were found and characterized. The structural results reported in the present study characterize one of the functional states of the enzyme fixed in the crystal structure.

AB - Laccase (oxygen oxidoreductase, EC 1.10.3.2) belongs to the multicopper oxidase family. The main function of this enzyme is to perform electron transfer from the oxidized substrate through the mononuclear copper-containing site T1 to the oxygen molecule bound to the site T3 in the trinuclear T2/T3 cluster. The structures of two new fungal laccases from C. maxima and C. zonatus were solved on the basis of synchrotron X-ray diffraction data. Both laccases show high structural homology with laccases from other sources. The role of the carbohydrate component of laccases in structure stabilization and formation of ordered protein crystals was demonstrated. In the structures of C. maxima and C. zonatus laccases, two water channels of functional importance were found and characterized. The structural results reported in the present study characterize one of the functional states of the enzyme fixed in the crystal structure.

KW - WHITE-ROT FUNGI

KW - CRYSTAL-STRUCTURE

KW - ANGSTROM RESOLUTION

KW - COPRINUS-CINEREUS

KW - ASCORBATE OXIDASE

KW - ELECTRON-TRANSFER

KW - FULL COMPLEMENT

KW - NITRIC-OXIDE

KW - LIGNIN

KW - SUBSTRATE

UR - http://www.scopus.com/inward/record.url?scp=34848818450&partnerID=8YFLogxK

U2 - 10.1134/S1063774507050124

DO - 10.1134/S1063774507050124

M3 - Article

SN - 1562-689X

VL - 52

SP - 826

EP - 837

JO - Crystallography Reports

JF - Crystallography Reports

ER -

Comparative analysis of spatial organization of laccases from Cerrena maxima and Coriolus zonatus

Abstract

Keywords

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