A new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes

Tutkimustuotos: Lehtiartikkelivertaisarvioitu

Tutkijat

Organisaatiot

  • University of Eastern Finland
  • VTT Technical Research Centre of Finland

Kuvaus

Coupled binuclear copper (CBC) enzymes have a conserved type 3 copper site that binds molecular oxygen to oxidize various mono- and diphenolic compounds. In this study, we found a new crystal form of catechol oxidase from Aspergillus oryzae (AoCO4) and solved two new structures from two different crystals at 1.8-Å and at 2.5-Å resolutions. These structures showed different copper site forms (met/deoxy and deoxy) and also differed from the copper site observed in the previously solved structure of AoCO4. We also analysed the electron density maps of all of the 56 CBC enzyme structures available in the protein data bank (PDB) and found that many of the published structures have vague copper sites. Some of the copper sites were then re-refined to find a better fit to the observed electron density. General problems in the refinement of metalloproteins and metal centres are discussed.

Yksityiskohdat

AlkuperäiskieliEnglanti
Artikkelie0196691
JulkaisuPloS one
Vuosikerta13
Numero5
TilaJulkaistu - 1 toukokuuta 2018
OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu

ID: 32865226