6QZO
Crystal structure of DyP-type peroxidase from Cellulomonas bogoriensis
Summary for 6QZO
| Entry DOI | 10.2210/pdb6qzo/pdb |
| Descriptor | Peroxidase, PROTOPORPHYRIN IX CONTAINING FE, TRIETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Cellulomonas bogoriensis 69B4 = DSM 16987 |
| Total number of polymer chains | 8 |
| Total formula weight | 336733.79 |
| Authors | Rozeboom, H.J.,Fraaije, M.W. (deposition date: 2019-03-12, release date: 2019-04-03, Last modification date: 2024-01-24) |
| Primary citation | Habib, M.H.,Rozeboom, H.J.,Fraaije, M.W. Characterization of a New DyP-Peroxidase from the Alkaliphilic Cellulomonad, Cellulomonas bogoriensis. Molecules, 24:-, 2019 Cited by PubMed Abstract: DyP-type peroxidases are heme-containing enzymes that have received increasing attention over recent years with regards to their potential as biocatalysts. A novel DyP-type peroxidase (DyP) was discovered from the alkaliphilic cellulomonad, , which could be overexpressed in . The biochemical characterization of the recombinant enzyme showed that it is a heme-containing enzyme capable to act as a peroxidase on several dyes. With the tested substrates, the enzyme is most active at acidic pH values and is quite tolerant towards solvents. The crystal structure of DyP was solved which revealed atomic details of the dimeric heme-containing enzyme. A peculiar feature of DyP is the presence of a glutamate in the active site which in most other DyPs is an aspartate, being part of the DyP-typifying sequence motif GXXDG. The E201D DyP mutant was prepared and analyzed which revealed that the mutant enzyme shows a significantly higher activity on several dyes when compared with the wild-type enzyme. PubMed: 30934796DOI: 10.3390/molecules24071208 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
