1mnp
From Proteopedia
MANGANESE PEROXIDASE
Structural highlights
Function[PEM1_PHACH] Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedManganese peroxidase from the white rot basidiomycete Phanerochaete chrysosporium has been crystallized in a form suitable for high-resolution X-ray structure determination. Crystals were grown from solutions containing 30% polyethylene glycol 8000, ammonium sulfate and cacodylate buffer at pH 6.5, using macroseeding techniques. A complete data set has been obtained to 2.06 A resolution. The data can be indexed in space group P1 with a = 45.96 A, b = 53.77 A, c = 84.87 A, alpha = 97.01 degrees, beta = 105.72 degrees and gamma = 90.1 degrees, with two peroxidase molecules per asymmetric unit, or in space group C2 with a = 163.23 A, b = 45.97 A, c = 53.72 A and beta = 97.16 degrees, with only one molecule in the assymetric unit. Lignin peroxidase, which shares about 57% sequence identity with manganese peroxidase, was used as a probe for molecular replacement. Unique rotation and translation solutions have been obtained in space groups P1 and C2. The structure has been partially refined in space group C2 to R = 0.22 for data between 10 and 2.06 A. Preliminary crystallographic analysis of manganese peroxidase from Phanerochaete chrysosporium.,Sundaramoorthy M, Kishi K, Gold MH, Poulos TL J Mol Biol. 1994 May 20;238(5):845-8. PMID:8182752[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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