1V10

Structure of Rigidoporus lignosus laccase from hemihedrally twinned crystals

1V10 の概要

• エントリーDOI: 10.2210/pdb1v10/pdb
• 分子名称: LACCASE, COPPER (II) ION (3 entities in total)
• 機能のキーワード: multicopper blue oxidase, oxidase
• 由来する生物種: RIGIDOPORUS LIGNOSUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55857.99

構造登録者

Rizzi, M.,Garavaglia, S.,Palmieri, F.,Cambria, A. (登録日: 2004-04-02, 公開日: 2004-09-16, 最終更新日: 2024-10-16)

主引用文献

Garavaglia, S.,Cambria, M.T.,Miglio, M.,Ragusa, S.,Iacobazzi, V.,Palmieri, F.,D'Ambrosio, C.,Scaloni, A.,Rizzi, M.
The Structure of Rigidoporus Lignosus Laccase Containing a Full Complement of Copper Ions, Reveals an Asymmetrical Arrangement for the T3 Copper Pair
J.Mol.Biol., 342:1519-, 2004

PubMed Abstract: Laccase is a multicopper blue oxidase that couples the four-electron reduction of oxygen with the oxidation of a broad range of organic substrates, including phenols and arylamines. The enzyme is the object of intense biotechnological research, due to its employment in bioremediation of soils and water as well as in other biotechnological applications. We report here the cDNA and protein sequences, the post-translational modifications, the crystallization and X-ray structure determination of a laccase from the white-rot fungus Rigidoporus lignosus. The amino acid residues sequence deduced from cDNA clearly identified a pre-sequence of 21 residues representing the signal for extra-cellular localization. Mass spectrometry analysis performed on the salvage enzyme, confirmed the deduced sequence and precisely mapped two glycosylation sites at Asn337 and Asn435, determining the nature of the bound glycosidic moieties. The crystal structure was determined at 1.7A resolution from perfectly hemihedrally twinned crystals, by molecular replacement technique. While the overall structure closely resembled those reported for other fungal laccases, the analysis of the T2/T3 trinuclear cluster revealed an unprecedented coordination sphere for the T3 copper pair. No bridging oxygen ligand was present between the two T3 copper ions, which were no longer symmetrically coordinated. The observed structure could represent an intermediate along the process of four-electron reduction of oxygen to water taking place at the trinuclear copper cluster.

PubMed: 15364578
DOI: 10.1016/J.JMB.2004.07.100

実験手法

X-RAY DIFFRACTION (1.7 Å)