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Crystallization and preliminary X-ray diffraction analysis of pyranose 2-oxidase from the white-rot fungus Trametes multicolor

Hällberg, B. Martin (author)
KTH,Bioteknologi
Leitner, Christian (author)
KTH,Bioteknologi
Haltrich, Dietmar (author)
KTH,Bioteknologi
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Divne, Christina (author)
KTH,Bioteknologi
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 (creator_code:org_t)
2003-12-18
2004
English.
In: Acta Crystallographica Section D. - : International Union of Crystallography (IUCr). - 0907-4449 .- 1399-0047. ; 60, s. 197-199
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Pyranose 2-oxidase (P2Ox) is a 270 kDa homotetrameric flavoenzyme that catalyzes the oxidation of D-glucose to 2-keto-D-glucose. P2Ox participates in lignin degradation by white-rot fungi and a tentative role of the enzyme is the production of H2O2 for lignin peroxidases. Crystals of Trametes multicolor P2Ox were grown from monomethylether PEG 2000, sodium acetate, MgCl2 and Ta6Br12. They belong to space group P2(1), with unit-cell parameters a = 99.9, b = 101.7, c = 135.6 Angstrom, beta = 90.85degrees. X-ray diffraction data to 2.0 Angstrom resolution were collected using synchrotron radiation. Self-rotation function calculations suggest that the asymmetric unit contains one homotetramer with 222 point-group symmetry.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Keyword

phanerochaete-chrysosporium
rotation function
crystal-structure
screening method
oxidase
proteins
versicolor
cultures
program

Publication and Content Type

ref (subject category)
art (subject category)

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