Crystallization and preliminary X-ray diffraction analysis of pyranose 2-oxidase from the white-rot fungus Trametes multicolor
2004 (English)In: Acta Crystallographica Section D: Biological Crystallography, ISSN 0907-4449, E-ISSN 1399-0047, Vol. 60, 197-199 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2004. Vol. 60, 197-199 p.
phanerochaete-chrysosporium, rotation function, crystal-structure, screening method, oxidase, proteins, versicolor, cultures, program
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:kth:diva-23033DOI: 10.1107/s0907444903024922ISI: 000187399200045ScopusID: 2-s2.0-4344667604OAI: oai:DiVA.org:kth-23033DiVA: diva2:341731
QC 20100525 QC 201111022010-08-102010-08-102011-11-02Bibliographically approved