5WHQ
Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.9 A
Summary for 5WHQ
| Entry DOI | 10.2210/pdb5whq/pdb |
| Related | 5WHS |
| Descriptor | Catalase-peroxidase, PROTOPORPHYRIN IX CONTAINING FE, POTASSIUM ION, ... (4 entities in total) |
| Functional Keywords | catalase-peroxidase, neurospora crassa, heme, hydrogen peroxide, oxidoreductase |
| Biological source | Neurospora crassa |
| Total number of polymer chains | 2 |
| Total formula weight | 171669.58 |
| Authors | Diaz-Vilchis, A.,Vega-Garcia, V.,Rudino-Pinera, E.,Hansberg, W. (deposition date: 2017-07-18, release date: 2018-01-17, Last modification date: 2024-11-13) |
| Primary citation | Vega-Garcia, V.,Diaz-Vilchis, A.,Saucedo-Vazquez, J.P.,Solano-Peralta, A.,Rudino-Pinera, E.,Hansberg, W. Structure, kinetics, molecular and redox properties of a cytosolic and developmentally regulated fungal catalase-peroxidase. Arch. Biochem. Biophys., 640:17-26, 2018 Cited by PubMed Abstract: CAT-2, a cytosolic catalase-peroxidase (CP) from Neurospora crassa, which is induced during asexual spore formation, was heterologously expressed and characterized. CAT-2 had the Met-Tyr-Trp (M-Y-W) adduct required for catalase activity. Its K for HO was micromolar for peroxidase and millimolar for catalase activity. A E = -158 mV reduction potential value was obtained and the Soret band shift suggested a mixture of low and high spin ferric iron. CAT-2 EPR spectrum at 10 K indicated an axial and a rhombic component. With peroxyacetic acid (PAA), formation of Compound I* was observed with EPR. CAT-2 homodimer crystallographic structure contained two K ions; Glu107 residues were displaced to bind them. CAT-2 showed the essential amino acid residues for activity in similar positions to other CPs. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 was oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other N. crassa enzymes that utilize HO as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to HO selection in water. PubMed: 29305053DOI: 10.1016/j.abb.2017.12.021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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