Structural highlights
4x4k is a 1 chain structure with sequence from Botrytis aclada. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 2.3Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
H8ZRU2_9HELO
Publication Abstract from PubMed
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.
Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada.,Osipov EM, Polyakov KM, Tikhonova TV, Kittl R, Dorovatovskii PV, Shleev SV, Popov VO, Ludwig R Acta Crystallogr F Struct Biol Commun. 2015 Dec 1;71(Pt 12):1465-9. doi:, 10.1107/S2053230X1502052X. Epub 2015 Nov 18. PMID:26625287[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Osipov EM, Polyakov KM, Tikhonova TV, Kittl R, Dorovatovskii PV, Shleev SV, Popov VO, Ludwig R. Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada. Acta Crystallogr F Struct Biol Commun. 2015 Dec 1;71(Pt 12):1465-9. doi:, 10.1107/S2053230X1502052X. Epub 2015 Nov 18. PMID:26625287 doi:http://dx.doi.org/10.1107/S2053230X1502052X
