A near atomic resolution structure of a Melanocarpus albomyces laccase

Nina Hakulinen (Corresponding Author), Martina Andberg, Johanna Kallio, Anu Koivula, Kristiina Kruus, Juha Rouvinen

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

We have solved a crystal structure from Melanocarpus albomyces laccase expressed in the filamentous fungus Trichoderma reesei (rMaL) at 1.3 Å resolution by using synchrotron radiation at 100 K. At the moment, this is the highest resolution that has been attained for any multicopper oxidase. The present structure confirmed our earlier proposal regarding the dynamic behaviour of the copper cluster. Thermal ellipsoids of copper atoms indicated movements of trinuclear site coppers. The direction of the type-3 copper motion was perpendicular to the type-2 copper. In addition, the structure at 1.3 Å resolution allowed us to describe important solvent cavities of the enzyme and the structure is also compared with other known multicopper oxidases. T2 and T3 solvent cavities, and a putative SDS-gate, formed by Ser142, Ser510 and the C-terminal Asp556 of rMaL, are described. We also observed a 2-oxohistidine, an oxidized histidine, possibly caused by a metal-catalysed oxidation by the trinuclear site coppers. To our knowledge, this is the first time that 2-oxohistidine has been observed in a protein crystal structure.

Original languageEnglish
Pages (from-to)29 - 39
Number of pages11
JournalJournal of Structural Biology
Volume162
Issue number1
DOIs
Publication statusPublished - 2008
MoE publication typeA1 Journal article-refereed

Fingerprint

Laccase
Copper
Oxidoreductases
Synchrotrons
Trichoderma
Histidine
Fungi
Hot Temperature
Metals
Radiation
Enzymes
Proteins

Keywords

  • laccase
  • multicopper oxidase
  • melanocarpus albomyces
  • 2-Oxo-histidine
  • SDS-gate
  • oxidases
  • Trichoderma reesei
  • filamentous fungi

Cite this

@article{be40430cf62b42ee97ef62a8050f5fb8,
title = "A near atomic resolution structure of a Melanocarpus albomyces laccase",
abstract = "We have solved a crystal structure from Melanocarpus albomyces laccase expressed in the filamentous fungus Trichoderma reesei (rMaL) at 1.3 {\AA} resolution by using synchrotron radiation at 100 K. At the moment, this is the highest resolution that has been attained for any multicopper oxidase. The present structure confirmed our earlier proposal regarding the dynamic behaviour of the copper cluster. Thermal ellipsoids of copper atoms indicated movements of trinuclear site coppers. The direction of the type-3 copper motion was perpendicular to the type-2 copper. In addition, the structure at 1.3 {\AA} resolution allowed us to describe important solvent cavities of the enzyme and the structure is also compared with other known multicopper oxidases. T2 and T3 solvent cavities, and a putative SDS-gate, formed by Ser142, Ser510 and the C-terminal Asp556 of rMaL, are described. We also observed a 2-oxohistidine, an oxidized histidine, possibly caused by a metal-catalysed oxidation by the trinuclear site coppers. To our knowledge, this is the first time that 2-oxohistidine has been observed in a protein crystal structure.",
keywords = "laccase, multicopper oxidase, melanocarpus albomyces, 2-Oxo-histidine, SDS-gate, oxidases, Trichoderma reesei, filamentous fungi",
author = "Nina Hakulinen and Martina Andberg and Johanna Kallio and Anu Koivula and Kristiina Kruus and Juha Rouvinen",
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language = "English",
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A near atomic resolution structure of a Melanocarpus albomyces laccase. / Hakulinen, Nina (Corresponding Author); Andberg, Martina; Kallio, Johanna; Koivula, Anu; Kruus, Kristiina; Rouvinen, Juha.

In: Journal of Structural Biology, Vol. 162, No. 1, 2008, p. 29 - 39.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - A near atomic resolution structure of a Melanocarpus albomyces laccase

AU - Hakulinen, Nina

AU - Andberg, Martina

AU - Kallio, Johanna

AU - Koivula, Anu

AU - Kruus, Kristiina

AU - Rouvinen, Juha

PY - 2008

Y1 - 2008

N2 - We have solved a crystal structure from Melanocarpus albomyces laccase expressed in the filamentous fungus Trichoderma reesei (rMaL) at 1.3 Å resolution by using synchrotron radiation at 100 K. At the moment, this is the highest resolution that has been attained for any multicopper oxidase. The present structure confirmed our earlier proposal regarding the dynamic behaviour of the copper cluster. Thermal ellipsoids of copper atoms indicated movements of trinuclear site coppers. The direction of the type-3 copper motion was perpendicular to the type-2 copper. In addition, the structure at 1.3 Å resolution allowed us to describe important solvent cavities of the enzyme and the structure is also compared with other known multicopper oxidases. T2 and T3 solvent cavities, and a putative SDS-gate, formed by Ser142, Ser510 and the C-terminal Asp556 of rMaL, are described. We also observed a 2-oxohistidine, an oxidized histidine, possibly caused by a metal-catalysed oxidation by the trinuclear site coppers. To our knowledge, this is the first time that 2-oxohistidine has been observed in a protein crystal structure.

AB - We have solved a crystal structure from Melanocarpus albomyces laccase expressed in the filamentous fungus Trichoderma reesei (rMaL) at 1.3 Å resolution by using synchrotron radiation at 100 K. At the moment, this is the highest resolution that has been attained for any multicopper oxidase. The present structure confirmed our earlier proposal regarding the dynamic behaviour of the copper cluster. Thermal ellipsoids of copper atoms indicated movements of trinuclear site coppers. The direction of the type-3 copper motion was perpendicular to the type-2 copper. In addition, the structure at 1.3 Å resolution allowed us to describe important solvent cavities of the enzyme and the structure is also compared with other known multicopper oxidases. T2 and T3 solvent cavities, and a putative SDS-gate, formed by Ser142, Ser510 and the C-terminal Asp556 of rMaL, are described. We also observed a 2-oxohistidine, an oxidized histidine, possibly caused by a metal-catalysed oxidation by the trinuclear site coppers. To our knowledge, this is the first time that 2-oxohistidine has been observed in a protein crystal structure.

KW - laccase

KW - multicopper oxidase

KW - melanocarpus albomyces

KW - 2-Oxo-histidine

KW - SDS-gate

KW - oxidases

KW - Trichoderma reesei

KW - filamentous fungi

U2 - 10.1016/j.jsb.2007.12.003

DO - 10.1016/j.jsb.2007.12.003

M3 - Article

VL - 162

SP - 29

EP - 39

JO - Journal of Structural Biology

JF - Journal of Structural Biology

SN - 1047-8477

IS - 1

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