4AUE

Crystal structure, recombinant expression and mutagenesis studies of the bifunctional catalase-phenol oxidase from Scytalidium thermophilum

Summary for 4AUE

• Entry DOI: 10.2210/pdb4aue/pdb
• Related: 4AUL 4AUM 4AUN 4B2Y 4B31 4B40
• Descriptor: CATALASE-PHENOL OXIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE, ... (6 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: SCYTALIDIUM THERMOPHILUM
• Total number of polymer chains: 4
• Total formula weight: 322321.71

Authors

Yuzugullu, Y.,Trinh, C.H.,Smith, M.A.,Pearson, A.R.,Phillips, S.E.V.,Sutay Kocabas, D.,Bakir, U.,Ogel, Z.B.,McPherson, M.J. (deposition date: 2012-05-17, release date: 2013-02-27, Last modification date: 2023-12-20)

Primary citation

Yuzugullu, Y.,Trinh, C.H.,Smith, M.A.,Pearson, A.R.,Phillips, S.E.V.,Sutay Kocabas, D.,Bakir, U.,Ogel, Z.B.,McPherson, M.J.
Structure, Recombinant Expression and Mutagenesis Studies of the Catalase with Oxidase Activity from Scytalidium Thermophilum
Acta Crystallogr.,Sect.D, 69:398-, 2013

PubMed Abstract: Scytalidium thermophilum produces a catalase with phenol oxidase activity (CATPO) that catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds. A codon-optimized catpo gene was cloned and expressed in Escherichia coli. The crystal structures of native and recombinant S. thermophilum CATPO and two variants, H82N and V123F, were determined at resolutions of 2.7, 1.4, 1.5 and 1.9 Å, respectively. The structure of CATPO reveals a homotetramer with 698 residues per subunit and with strong structural similarity to Penicillium vitale catalase. The haem component is cis-hydroxychlorin γ-spirolactone, which is rotated 180° with respect to small-subunit catalases. The haem-binding pocket contains two highly conserved water molecules on the distal side. The H82N mutation resulted in conversion of the native d-type haem to a b-type haem. Kinetic studies of the H82N and V123F mutants indicate that both activities are likely to be associated with the haem centre and suggest that the secondary oxidase activity may be a general feature of catalases in the absence of hydrogen peroxide.

PubMed: 23519415
DOI: 10.1107/S0907444912049001

Experimental method

X-RAY DIFFRACTION (2.7 Å)