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Structure paper

TitleThe Role of Asp116 in the Reductive Cleavage of Dioxygen to Water in Cota Laccase: Assistance During the Proton Transfer Mechanism
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 68, Page 186-, Year 2012
Publish dateOct 31, 2011 (structure data deposition date)
AuthorsSilva, C.S. / Damas, J.M. / Chen, Z. / Brissos, V. / Martins, L.O. / Soares, C.M. / Lindley, P.F. / Bento, I.
External linksActa Crystallogr. ,Sect. D / PubMed:22281748
MethodsX-ray diffraction
Resolution1.95 - 2.1 Å
Structure data

PDB-4a66:
Mutations in the neighbourhood of CotA-laccase trinuclear site: D116A mutant
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-4a67:
Mutations in the neighbourhood of CotA-laccase trinuclear site: D116E mutant
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4a68:
Mutations in the neighbourhood of CotA-laccase trinuclear site: D116N mutant
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PER:
PEROXIDE ION

ChemComp-HOH:
WATER

ChemComp-OH:
HYDROXIDE ION

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

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

Source
  • bacillus subtilis (bacteria)
KeywordsOXIDOREDUCTASE / MULTI-COPPER OXIDASE / OXIDOREDUCTASE ACTIVITY / TRINUCLEAR CLUSTER / DIOXYGEN REDUCTION

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