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2Q9O

Near-atomic resolution structure of a Melanocarpus albomyces laccase

Summary for 2Q9O
Entry DOI10.2210/pdb2q9o/pdb
Related1gw0 2ih8 2ih9
DescriptorLaccase-1, GLYCEROL, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
Functional Keywordslaccase, multicopper oxidase, melanocarpus albomyces, 2-oxohistidine, oxidoreductase
Biological sourceMelanocarpus albomyces
Total number of polymer chains2
Total formula weight131833.93
Authors
Hakulinen, N.,Rouvinen, J. (deposition date: 2007-06-13, release date: 2008-03-25, Last modification date: 2020-07-29)
Primary citationHakulinen, N.,Andberg, M.,Kallio, J.,Koivula, A.,Kruus, K.,Rouvinen, J.
A near atomic resolution structure of a Melanocarpus albomyces laccase.
J.Struct.Biol., 162:29-39, 2008
Cited by
PubMed Abstract: We have solved a crystal structure from Melanocarpus albomyces laccase expressed in the filamentous fungus Trichoderma reesei (rMaL) at 1.3A resolution by using synchrotron radiation at 100K. At the moment, this is the highest resolution that has been attained for any multicopper oxidase. The present structure confirmed our earlier proposal regarding the dynamic behaviour of the copper cluster. Thermal ellipsoids of copper atoms indicated movements of trinuclear site coppers. The direction of the type-3 copper motion was perpendicular to the type-2 copper. In addition, the structure at 1.3A resolution allowed us to describe important solvent cavities of the enzyme and the structure is also compared with other known multicopper oxidases. T2 and T3 solvent cavities, and a putative SDS-gate, formed by Ser142, Ser510 and the C-terminal Asp556 of rMaL, are described. We also observed a 2-oxohistidine, an oxidized histidine, possibly caused by a metal-catalysed oxidation by the trinuclear site coppers. To our knowledge, this is the first time that 2-oxohistidine has been observed in a protein crystal structure.
PubMed: 18249560
DOI: 10.1016/j.jsb.2007.12.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.3 Å)
Structure validation

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