Crystal structure of an ascomycete fungal laccase from Thielavia arenaria 

Common structural features of asco-laccases

J.P. Kallio, C. Gasparetti, M. Andberg, H. Boer, A. Koivula, K. Kruus, J. Rouvinen, N. Hakulinen

Research output: Contribution to journalArticleScientificpeer-review

42 Citations (Scopus)

Abstract

Laccases are copper‐containing enzymes used in various applications, such as textile bleaching. Several crystal structures of laccases from fungi and bacteria are available, but ascomycete types of fungal laccases (asco‐laccases) have been rather unexplored, and to date only the crystal structure of Melanocarpusalbomyces laccase (MaL) has been published. We have now solved the crystal structure of another asco‐laccase, from Thielavia arenaria (TaLcc1), at 2.5 Å resolution. The loops near the T1 copper, forming the substrate‐binding pockets of the two asco‐laccases, differ to some extent, and include the amino acid thought to be responsible for catalytic proton transfer, which is Asp in TaLcc1, and Glu in MaL. In addition, the crystal structure of TaLcc1 does not have a chloride attached to the T2 copper, as observed in the crystal structure of MaL. The unique feature of TaLcc1 and MaL as compared with other laccases structures is that, in both structures, the processed C‐terminus blocks the T3 solvent channel leading towards the trinuclear centre, suggesting a common functional role for this conserved ‘C‐terminal plug’. We propose that the asco‐laccases utilize the C‐terminal carboxylic group in proton transfer processes, as has been suggested for Glu498 in the CotA laccase from Bacillus subtilis. The crystal structure of TaLcc1 also shows the formation of a similar weak homodimer, as observed for MaL, that may determine the properties of these asco‐laccases at high protein concentrations.
Original languageEnglish
Pages (from-to)2283-2295
Number of pages14
JournalFEBS Journal
Volume278
Issue number13
DOIs
Publication statusPublished - 2011
MoE publication typeA1 Journal article-refereed

Fingerprint

Fungal Structures
Laccase
Ascomycota
Crystal structure
Proton transfer
Protons
Copper
Textiles
Bacilli
Bleaching

Keywords

  • ascomycete
  • C-terminal plug
  • laccase
  • proton transfer
  • redox potential

Cite this

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title = "Crystal structure of an ascomycete fungal laccase from Thielavia arenaria : Common structural features of asco-laccases",
abstract = "Laccases are copper‐containing enzymes used in various applications, such as textile bleaching. Several crystal structures of laccases from fungi and bacteria are available, but ascomycete types of fungal laccases (asco‐laccases) have been rather unexplored, and to date only the crystal structure of Melanocarpus albomyces laccase (MaL) has been published. We have now solved the crystal structure of another asco‐laccase, from Thielavia arenaria (TaLcc1), at 2.5 {\AA} resolution. The loops near the T1 copper, forming the substrate‐binding pockets of the two asco‐laccases, differ to some extent, and include the amino acid thought to be responsible for catalytic proton transfer, which is Asp in TaLcc1, and Glu in MaL. In addition, the crystal structure of TaLcc1 does not have a chloride attached to the T2 copper, as observed in the crystal structure of MaL. The unique feature of TaLcc1 and MaL as compared with other laccases structures is that, in both structures, the processed C‐terminus blocks the T3 solvent channel leading towards the trinuclear centre, suggesting a common functional role for this conserved ‘C‐terminal plug’. We propose that the asco‐laccases utilize the C‐terminal carboxylic group in proton transfer processes, as has been suggested for Glu498 in the CotA laccase from Bacillus subtilis. The crystal structure of TaLcc1 also shows the formation of a similar weak homodimer, as observed for MaL, that may determine the properties of these asco‐laccases at high protein concentrations.",
keywords = "ascomycete, C-terminal plug, laccase, proton transfer, redox potential",
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Crystal structure of an ascomycete fungal laccase from Thielavia arenaria  : Common structural features of asco-laccases. / Kallio, J.P.; Gasparetti, C.; Andberg, M.; Boer, H.; Koivula, A.; Kruus, K.; Rouvinen, J.; Hakulinen, N.

In: FEBS Journal, Vol. 278, No. 13, 2011, p. 2283-2295.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Crystal structure of an ascomycete fungal laccase from Thielavia arenaria 

T2 - Common structural features of asco-laccases

AU - Kallio, J.P.

AU - Gasparetti, C.

AU - Andberg, M.

AU - Boer, H.

AU - Koivula, A.

AU - Kruus, K.

AU - Rouvinen, J.

AU - Hakulinen, N.

PY - 2011

Y1 - 2011

N2 - Laccases are copper‐containing enzymes used in various applications, such as textile bleaching. Several crystal structures of laccases from fungi and bacteria are available, but ascomycete types of fungal laccases (asco‐laccases) have been rather unexplored, and to date only the crystal structure of Melanocarpus albomyces laccase (MaL) has been published. We have now solved the crystal structure of another asco‐laccase, from Thielavia arenaria (TaLcc1), at 2.5 Å resolution. The loops near the T1 copper, forming the substrate‐binding pockets of the two asco‐laccases, differ to some extent, and include the amino acid thought to be responsible for catalytic proton transfer, which is Asp in TaLcc1, and Glu in MaL. In addition, the crystal structure of TaLcc1 does not have a chloride attached to the T2 copper, as observed in the crystal structure of MaL. The unique feature of TaLcc1 and MaL as compared with other laccases structures is that, in both structures, the processed C‐terminus blocks the T3 solvent channel leading towards the trinuclear centre, suggesting a common functional role for this conserved ‘C‐terminal plug’. We propose that the asco‐laccases utilize the C‐terminal carboxylic group in proton transfer processes, as has been suggested for Glu498 in the CotA laccase from Bacillus subtilis. The crystal structure of TaLcc1 also shows the formation of a similar weak homodimer, as observed for MaL, that may determine the properties of these asco‐laccases at high protein concentrations.

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KW - proton transfer

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