3qpk | pdb_00003qpk

Probing oxygen channels in Melanocarpus albomyces laccase

spinqualitylabelsall models 3qpk, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qpk is a 2 chain structure with sequence from Melanocarpus albomyces. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: CL, CU, NAG, SO4, XE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LAC1_MELAO Lignin degradation and detoxification of lignin-derived products (Probable). Publication Abstract from PubMed Laccases catalyze the oxidation of phenolic substrates and the concominant reduction of dioxygen to water. We used xenon as an oxygen probe in search of routes for the entry of dioxygen into the catalytic center. Two xenon-pressurized crystal structures of recombinant Melanocarpus albomyces laccase were determined, showing three hydrophobic Xe-binding sites located in domain C. The analysis of hydrophobic cavities in other laccase structures further suggested the preference of domain C for binding of hydrophobic species such as dioxygen, thus suggesting that the hydrophobic core of domain C could function as a channel through which dioxygen can enter the trinuclear copper center. Probing the Dioxygen Route in Melanocarpus albomyces Laccase with Pressurized Xenon Gas.,Kallio JP, Rouvinen J, Kruus K, Hakulinen N Biochemistry. 2011 May 5. PMID:21524088 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laccase 3D structures

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