1MNP

MANGANESE PEROXIDASE

Summary for 1MNP

• Entry DOI: 10.2210/pdb1mnp/pdb
• Descriptor: MANGANESE PEROXIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: heme peroxidase, peroxidase (donor: h2o2 oxidoreductase)
• Biological source: Phanerochaete chrysosporium
• Cellular location: Secreted: Q02567
• Total number of polymer chains: 1
• Total formula weight: 38658.96

Authors

Sundaramoorthy, M.,Poulos, T.L. (deposition date: 1995-01-27, release date: 1995-09-15, Last modification date: 2024-11-13)

Primary citation

Sundaramoorthy, M.,Kishi, K.,Gold, M.H.,Poulos, T.L.
Preliminary crystallographic analysis of manganese peroxidase from Phanerochaete chrysosporium.
J.Mol.Biol., 238:845-848, 1994

PubMed Abstract: 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.

PubMed: 8182752
DOI: 10.1006/jmbi.1994.1338

Experimental method

X-RAY DIFFRACTION (2 Å)