4X4K

Structure of laccase from Botrytis aclada with full copper content

Summary for 4X4K

• Entry DOI: 10.2210/pdb4x4k/pdb
• Related: 3sqr
• Descriptor: Laccase, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: laccase, cu(i) complex, full copper content, balbes nmr, metal binding protein
• Biological source: Botrytis aclada
• Total number of polymer chains: 1
• Total formula weight: 67028.56

Authors

Osipov, E.M.,Polyakov, K.M.,Tikhonova, T.V.,Kittl, R.,Shleev, S.V.,Ludwig, R.,Popov, V.O. (deposition date: 2014-12-03, release date: 2015-12-09, Last modification date: 2024-01-10)

Primary citation

Osipov, E.M.,Polyakov, K.M.,Tikhonova, T.V.,Kittl, R.,Dorovatovskii, P.V.,Shleev, S.V.,Popov, V.O.,Ludwig, R.
Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada.
Acta Crystallogr.,Sect.F, 71:1465-1469, 2015

PubMed Abstract: Laccases belong to the class of multicopper oxidases catalyzing the oxidation of phenols accompanied by the reduction of molecular oxygen to water without the formation of hydrogen peroxide. The activity of laccases depends on the number of Cu atoms per enzyme molecule. The structure of type 2 copper-depleted laccase from Botrytis aclada has been solved previously. With the aim of obtaining the structure of the native form of the enzyme, crystals of the depleted laccase were soaked in Cu(+)- and Cu(2+)-containing solutions. Copper ions were found to be incorporated into the active site only when Cu(+) was used. A comparative analysis of the native and depleted forms of the enzymes was performed.

PubMed: 26625287
DOI: 10.1107/S2053230X1502052X

Experimental method

X-RAY DIFFRACTION (2.3 Å)