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TitleElucidation of the crystal structure of Coriolopsis caperata laccase: restoration of the structure and activity of the native enzyme from the T2-depleted form by copper ions.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 71, Page 854-861, Year 2015
Publish dateMar 5, 2013 (structure data deposition date)
AuthorsGlazunova, O.A. / Polyakov, K.M. / Fedorova, T.V. / Dorovatovskii, P.V. / Koroleva, O.V.
External linksActa Crystallogr. ,Sect. D / PubMed:25849396
MethodsX-ray diffraction
Resolution1.6 - 1.89 Å
Structure data

PDB-4jhu:
T2-depleted laccase from Coriolopsis caperata soaked with CuCl
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

PDB-4jhv:
T2-depleted laccase from Coriolopsis caperata
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-PG6:
1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

Source
  • coriolopsis caperata (fungus)
KeywordsOXIDOREDUCTASE / BETA SHEET / 4-COPPER PROTEIN / METAL-BINDING / LACCASE

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