5ZZ1
Probing the active center of catalase-phenol oxidase from Scytalidium thermophilum
Summary for 5ZZ1
| Entry DOI | 10.2210/pdb5zz1/pdb |
| Descriptor | Catalase, CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE, 3-AMINO-1,2,4-TRIAZOLE, ... (5 entities in total) |
| Functional Keywords | catalase-phenol oxidase, scytalidium thermophilum, oxidoreductase |
| Biological source | Mycothermus thermophilus |
| Total number of polymer chains | 4 |
| Total formula weight | 320526.45 |
| Authors | Yuzugullu Karakus, Y.,Trinh, C.H.,Pearson, A.R.,Ogel, Z.B.,McPherson, M.J. (deposition date: 2018-05-29, release date: 2019-05-29, Last modification date: 2023-11-22) |
| Primary citation | Yuzugullu Karakus, Y.,Goc, G.,Balci, S.,Yorke, B.A.,Trinh, C.H.,McPherson, M.J.,Pearson, A.R. Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase. Acta Crystallogr D Struct Biol, 74:979-985, 2018 Cited by PubMed Abstract: The catalase from Scytalidium thermophilum is a homotetramer containing a heme d in each active site. Although the enzyme has a classical monofunctional catalase fold, it also possesses oxidase activity towards a number of small organics, including catechol and phenol. In order to further investigate this, the crystal structure of the complex of the catalase with the classical catalase inhibitor 3-amino-1,2,4-triazole (3TR) was determined at 1.95 Å resolution. Surprisingly, no binding to the heme site was observed; instead, 3TR occupies a binding site corresponding to the NADPH-binding pocket in mammalian catalases at the entrance to a lateral channel leading to the heme. Kinetic analysis of site-directed mutants supports the assignment of this pocket as the binding site for oxidase substrates. PubMed: 30289408DOI: 10.1107/S2059798318010628 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
Download full validation report
