1mnp

OverviewOverview

Manganese 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.

About this StructureAbout this Structure

1MNP is a Single protein structure of sequence from Phanerochaete chrysosporium with CA, MN and HEM as ligands. Active as Peroxidase, with EC number 1.11.1.7 Full crystallographic information is available from OCA.

ReferenceReference

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

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