3QPK

Probing oxygen channels in Melanocarpus albomyces laccase

Summary for 3QPK

• Entry DOI: 10.2210/pdb3qpk/pdb
• Related: 1GW0 2IH8 2IH9 2Q9O 3DKH 3FU7 3FU8 3FU9 3PPS
• Descriptor: Laccase-1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (8 entities in total)
• Functional Keywords: cu binding, xe binding, laccase, multicopper oxidase, oxidoreductase
• Biological source: Melanocarpus albomyces
• Total number of polymer chains: 2
• Total formula weight: 129326.89

Authors

Kallio, J.P.,Rouvinen, J.,Hakulinen, N. (deposition date: 2011-02-14, release date: 2011-05-11, Last modification date: 2024-11-06)

Primary citation

Kallio, J.P.,Rouvinen, J.,Kruus, K.,Hakulinen, N.
Probing the Dioxygen Route in Melanocarpus albomyces Laccase with Pressurized Xenon Gas.
Biochemistry, 50:4396-4398, 2011

PubMed Abstract: 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.

PubMed: 21524088
DOI: 10.1021/bi200486b

Experimental method

X-RAY DIFFRACTION (1.9 Å)