Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site

Nina Hakulinen, Laura-Leena Kiiskinen, Kristiina Kruus, Markku Saloheimo, Arja Paananen, Anu Koivula, Juha Rouvinen (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

286 Citations (Scopus)

Abstract

We have crystallized the ascomycete laccase from Melanocarpus albomyces with all four coppers present and determined the crystal structure at 2.4 Å resolution. The enzyme is heavily glycosylated and consists of three cupredoxin-like domains, similar to those found in the Cu-depleted basidiomycete laccase from Coprinus cinereus. However, there are significant differences in the loops forming the substrate-binding pocket. In addition, the crystal structure of the M. albomyces laccase revealed elongated electron density between all three coppers in the trinuclear copper site, suggesting that an oxygen molecule binds with a novel geometry. This oxygen, required in the reaction, may enter the trinuclear site through the tunnel, which is open in the structure of the C. cinereus laccase. In contrast, the C-terminus on the M. albomyces laccase forms a plug that blocks this access.
Original languageEnglish
Pages (from-to)601-605
JournalNature Structural Biology
Volume9
Issue number8
DOIs
Publication statusPublished - 2002
MoE publication typeA1 Journal article-refereed

Fingerprint

Laccase
Copper
Coprinus
Oxygen
Basidiomycota
Ascomycota
Electrons
Enzymes

Keywords

  • laccase
  • Melanocarpus albomyces laccase
  • crystal structure
  • Melanocarpus albomyces

Cite this

@article{485e5cb4bf7b44b4a197247d3817caea,
title = "Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site",
abstract = "We have crystallized the ascomycete laccase from Melanocarpus albomyces with all four coppers present and determined the crystal structure at 2.4 {\AA} resolution. The enzyme is heavily glycosylated and consists of three cupredoxin-like domains, similar to those found in the Cu-depleted basidiomycete laccase from Coprinus cinereus. However, there are significant differences in the loops forming the substrate-binding pocket. In addition, the crystal structure of the M. albomyces laccase revealed elongated electron density between all three coppers in the trinuclear copper site, suggesting that an oxygen molecule binds with a novel geometry. This oxygen, required in the reaction, may enter the trinuclear site through the tunnel, which is open in the structure of the C. cinereus laccase. In contrast, the C-terminus on the M. albomyces laccase forms a plug that blocks this access.",
keywords = "laccase, Melanocarpus albomyces laccase, crystal structure, Melanocarpus albomyces",
author = "Nina Hakulinen and Laura-Leena Kiiskinen and Kristiina Kruus and Markku Saloheimo and Arja Paananen and Anu Koivula and Juha Rouvinen",
year = "2002",
doi = "10.1038/nsb823",
language = "English",
volume = "9",
pages = "601--605",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "8",

}

Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site. / Hakulinen, Nina; Kiiskinen, Laura-Leena; Kruus, Kristiina; Saloheimo, Markku; Paananen, Arja; Koivula, Anu; Rouvinen, Juha (Corresponding Author).

In: Nature Structural Biology, Vol. 9, No. 8, 2002, p. 601-605.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site

AU - Hakulinen, Nina

AU - Kiiskinen, Laura-Leena

AU - Kruus, Kristiina

AU - Saloheimo, Markku

AU - Paananen, Arja

AU - Koivula, Anu

AU - Rouvinen, Juha

PY - 2002

Y1 - 2002

N2 - We have crystallized the ascomycete laccase from Melanocarpus albomyces with all four coppers present and determined the crystal structure at 2.4 Å resolution. The enzyme is heavily glycosylated and consists of three cupredoxin-like domains, similar to those found in the Cu-depleted basidiomycete laccase from Coprinus cinereus. However, there are significant differences in the loops forming the substrate-binding pocket. In addition, the crystal structure of the M. albomyces laccase revealed elongated electron density between all three coppers in the trinuclear copper site, suggesting that an oxygen molecule binds with a novel geometry. This oxygen, required in the reaction, may enter the trinuclear site through the tunnel, which is open in the structure of the C. cinereus laccase. In contrast, the C-terminus on the M. albomyces laccase forms a plug that blocks this access.

AB - We have crystallized the ascomycete laccase from Melanocarpus albomyces with all four coppers present and determined the crystal structure at 2.4 Å resolution. The enzyme is heavily glycosylated and consists of three cupredoxin-like domains, similar to those found in the Cu-depleted basidiomycete laccase from Coprinus cinereus. However, there are significant differences in the loops forming the substrate-binding pocket. In addition, the crystal structure of the M. albomyces laccase revealed elongated electron density between all three coppers in the trinuclear copper site, suggesting that an oxygen molecule binds with a novel geometry. This oxygen, required in the reaction, may enter the trinuclear site through the tunnel, which is open in the structure of the C. cinereus laccase. In contrast, the C-terminus on the M. albomyces laccase forms a plug that blocks this access.

KW - laccase

KW - Melanocarpus albomyces laccase

KW - crystal structure

KW - Melanocarpus albomyces

U2 - 10.1038/nsb823

DO - 10.1038/nsb823

M3 - Article

VL - 9

SP - 601

EP - 605

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 8

ER -