5or3 | pdb_00005or3

Crystal structure of Aspergillus oryzae catechol oxidase in met/deoxy-form

spinqualitylabelsall models 5or3, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5or3 is a 4 chain structure with sequence from Aspergillus oryzae RIB40. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.795Å Ligands: BMA, CU, EDO, FLC, MAN, NAG, PER Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2UNF9_ASPOR Publication Abstract from PubMed 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-A and at 2.5-A 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. A new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes.,Penttinen L, Rutanen C, Saloheimo M, Kruus K, Rouvinen J, Hakulinen N PLoS One. 2018 May 1;13(5):e0196691. doi: 10.1371/journal.pone.0196691., eCollection 2018. PMID:29715329 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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