X-ray structural studies of the fungal laccase from Cerrena maxima

Andrey V. Lyashenko; Isabel Bento; Viatcheslav N. Zaitsev; Nadezhda E. Zhukhlistova; Yuliya N. Zhukova; Azat G. Gabdoulkhakov; Fkaterina Y. Morgunova; Wolfgang Voelter; Galina S. Kachalova; Elena V. Stepanova; Ga V. Koroleva; Victor S. Lamzin; Vladimir I. Tishkov; Christian Betzel; Peter F. Lindley; Al'bert M. Mikhailov

doi:10.1007/s00775-006-0158-x

X-ray structural studies of the fungal laccase from Cerrena maxima

Andrey V. Lyashenko, Isabel Bento, Viatcheslav N. Zaitsev, Nadezhda E. Zhukhlistova, Yuliya N. Zhukova, Azat G. Gabdoulkhakov, Fkaterina Y. Morgunova, Wolfgang Voelter, Galina S. Kachalova, Elena V. Stepanova, Ga V. Koroleva, Victor S. Lamzin, Vladimir I. Tishkov, Christian Betzel, Peter F. Lindley, Al'bert M. Mikhailov

School of Chemistry

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

Abstract

Laccases are members of the blue multicopper oxidase family. These enzymes oxidize substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and following the transfer of four electrons is reduced to two molecules of water. The X-ray structure of a laccase from Cerrena maxima has been elucidated at 1.9 angstrom resolution using synchrotron data and the molecular replacement technique. The final refinement coefficients are R-cryst = 16.8% and R-free = 23.0%, with root mean square deviations on bond lengths and bond angles of 0.015 angstrom and 1.51 degrees, respectively. The type 1 copper centre has an isoleucine residue at the axial position and the "resting" state of the trinuclear centre comprises a single oxygen (OH) moiety asymmetrically disposed between the two type 3 copper ions and a water molecule attached to the type 2 ion. Several carbohydrate binding sites have been identified and the glycan chains appear to promote the formation of well-ordered crystals. Two tyrosine residues near the protein surface have been found in a nitrated state.

Original language	English
Pages (from-to)	963-973
Number of pages	11
Journal	Journal of Biological Inorganic Chemistry
Volume	11
DOIs	https://doi.org/10.1007/s00775-006-0158-x
Publication status	Published - Nov 2006

Keywords

laccase
trinuclear copper site
glycans
nitrated tyrosine residues
WHITE-ROT FUNGI
CRYSTAL-STRUCTURE
ANGSTROM RESOLUTION
COPRINUS-CINEREUS
CORIOLUS-HIRSUTUS
ELECTRON-TRANSFER
FULL COMPLEMENT
COPPER PROTEINS
NITRIC-OXIDE
REDUCTION

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Lyashenko, A. V., Bento, I., Zaitsev, V. N., Zhukhlistova, N. E., Zhukova, Y. N., Gabdoulkhakov, A. G., Morgunova, F. Y., Voelter, W., Kachalova, G. S., Stepanova, E. V., Koroleva, G. V., Lamzin, V. S., Tishkov, V. I., Betzel, C., Lindley, P. F., & Mikhailov, A. M. (2006). X-ray structural studies of the fungal laccase from Cerrena maxima. Journal of Biological Inorganic Chemistry, 11, 963-973. https://doi.org/10.1007/s00775-006-0158-x

@article{708c08d9813742f8b27b1b7bfa5bd4d7,

title = "X-ray structural studies of the fungal laccase from Cerrena maxima",

abstract = "Laccases are members of the blue multicopper oxidase family. These enzymes oxidize substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and following the transfer of four electrons is reduced to two molecules of water. The X-ray structure of a laccase from Cerrena maxima has been elucidated at 1.9 angstrom resolution using synchrotron data and the molecular replacement technique. The final refinement coefficients are R-cryst = 16.8% and R-free = 23.0%, with root mean square deviations on bond lengths and bond angles of 0.015 angstrom and 1.51 degrees, respectively. The type 1 copper centre has an isoleucine residue at the axial position and the {"}resting{"} state of the trinuclear centre comprises a single oxygen (OH) moiety asymmetrically disposed between the two type 3 copper ions and a water molecule attached to the type 2 ion. Several carbohydrate binding sites have been identified and the glycan chains appear to promote the formation of well-ordered crystals. Two tyrosine residues near the protein surface have been found in a nitrated state.",

keywords = "laccase, trinuclear copper site, glycans, nitrated tyrosine residues, WHITE-ROT FUNGI, CRYSTAL-STRUCTURE, ANGSTROM RESOLUTION, COPRINUS-CINEREUS, CORIOLUS-HIRSUTUS, ELECTRON-TRANSFER, FULL COMPLEMENT, COPPER PROTEINS, NITRIC-OXIDE, REDUCTION",

author = "Lyashenko, {Andrey V.} and Isabel Bento and Zaitsev, {Viatcheslav N.} and Zhukhlistova, {Nadezhda E.} and Zhukova, {Yuliya N.} and Gabdoulkhakov, {Azat G.} and Morgunova, {Fkaterina Y.} and Wolfgang Voelter and Kachalova, {Galina S.} and Stepanova, {Elena V.} and Koroleva, {Ga V.} and Lamzin, {Victor S.} and Tishkov, {Vladimir I.} and Christian Betzel and Lindley, {Peter F.} and Mikhailov, {Al'bert M.}",

year = "2006",

month = nov,

doi = "10.1007/s00775-006-0158-x",

language = "English",

volume = "11",

pages = "963--973",

journal = "Journal of Biological Inorganic Chemistry",

issn = "0949-8257",

publisher = "Springer-Verlag",

}

Lyashenko, AV, Bento, I, Zaitsev, VN, Zhukhlistova, NE, Zhukova, YN, Gabdoulkhakov, AG, Morgunova, FY, Voelter, W, Kachalova, GS, Stepanova, EV, Koroleva, GV, Lamzin, VS, Tishkov, VI, Betzel, C, Lindley, PF & Mikhailov, AM 2006, 'X-ray structural studies of the fungal laccase from Cerrena maxima', Journal of Biological Inorganic Chemistry, vol. 11, pp. 963-973. https://doi.org/10.1007/s00775-006-0158-x

TY - JOUR

T1 - X-ray structural studies of the fungal laccase from Cerrena maxima

AU - Lyashenko, Andrey V.

AU - Bento, Isabel

AU - Zaitsev, Viatcheslav N.

AU - Zhukhlistova, Nadezhda E.

AU - Zhukova, Yuliya N.

AU - Gabdoulkhakov, Azat G.

AU - Morgunova, Fkaterina Y.

AU - Voelter, Wolfgang

AU - Kachalova, Galina S.

AU - Stepanova, Elena V.

AU - Koroleva, Ga V.

AU - Lamzin, Victor S.

AU - Tishkov, Vladimir I.

AU - Betzel, Christian

AU - Lindley, Peter F.

AU - Mikhailov, Al'bert M.

PY - 2006/11

Y1 - 2006/11

N2 - Laccases are members of the blue multicopper oxidase family. These enzymes oxidize substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and following the transfer of four electrons is reduced to two molecules of water. The X-ray structure of a laccase from Cerrena maxima has been elucidated at 1.9 angstrom resolution using synchrotron data and the molecular replacement technique. The final refinement coefficients are R-cryst = 16.8% and R-free = 23.0%, with root mean square deviations on bond lengths and bond angles of 0.015 angstrom and 1.51 degrees, respectively. The type 1 copper centre has an isoleucine residue at the axial position and the "resting" state of the trinuclear centre comprises a single oxygen (OH) moiety asymmetrically disposed between the two type 3 copper ions and a water molecule attached to the type 2 ion. Several carbohydrate binding sites have been identified and the glycan chains appear to promote the formation of well-ordered crystals. Two tyrosine residues near the protein surface have been found in a nitrated state.

AB - Laccases are members of the blue multicopper oxidase family. These enzymes oxidize substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and following the transfer of four electrons is reduced to two molecules of water. The X-ray structure of a laccase from Cerrena maxima has been elucidated at 1.9 angstrom resolution using synchrotron data and the molecular replacement technique. The final refinement coefficients are R-cryst = 16.8% and R-free = 23.0%, with root mean square deviations on bond lengths and bond angles of 0.015 angstrom and 1.51 degrees, respectively. The type 1 copper centre has an isoleucine residue at the axial position and the "resting" state of the trinuclear centre comprises a single oxygen (OH) moiety asymmetrically disposed between the two type 3 copper ions and a water molecule attached to the type 2 ion. Several carbohydrate binding sites have been identified and the glycan chains appear to promote the formation of well-ordered crystals. Two tyrosine residues near the protein surface have been found in a nitrated state.

KW - laccase

KW - trinuclear copper site

KW - glycans

KW - nitrated tyrosine residues

KW - WHITE-ROT FUNGI

KW - CRYSTAL-STRUCTURE

KW - ANGSTROM RESOLUTION

KW - COPRINUS-CINEREUS

KW - CORIOLUS-HIRSUTUS

KW - ELECTRON-TRANSFER

KW - FULL COMPLEMENT

KW - COPPER PROTEINS

KW - NITRIC-OXIDE

KW - REDUCTION

UR - http://www.scopus.com/inward/record.url?scp=33751209488&partnerID=8YFLogxK

U2 - 10.1007/s00775-006-0158-x

DO - 10.1007/s00775-006-0158-x

M3 - Article

SN - 0949-8257

VL - 11

SP - 963

EP - 973

JO - Journal of Biological Inorganic Chemistry

JF - Journal of Biological Inorganic Chemistry

ER -

X-ray structural studies of the fungal laccase from Cerrena maxima

Abstract

Keywords

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