8QX0
Ligninolytic manganese peroxidase Ape-MnP1 from Agaricales mushrooms in complex with a manganese ion
Summary for 8QX0
| Entry DOI | 10.2210/pdb8qx0/pdb |
| Descriptor | Peroxidase, MANGANESE (II) ION, PROTOPORPHYRIN IX CONTAINING FE, ... (7 entities in total) |
| Functional Keywords | manganese peroxidase, fungal, ligninolytic, oxidoreductase |
| Biological source | Agrocybe pediades |
| Total number of polymer chains | 1 |
| Total formula weight | 36087.44 |
| Authors | Santillana, E.,Romero, A. (deposition date: 2023-10-20, release date: 2024-06-26, Last modification date: 2024-11-13) |
| Primary citation | Sanchez-Ruiz, M.I.,Santillana, E.,Linde, D.,Romero, A.,Martinez, A.T.,Ruiz-Duenas, F.J. Structure-function characterization of two enzymes from novel subfamilies of manganese peroxidases secreted by the lignocellulose-degrading Agaricales fungi Agrocybe pediades and Cyathus striatus. Biotechnol Biofuels Bioprod, 17:74-74, 2024 Cited by PubMed Abstract: Manganese peroxidases (MnPs) are, together with lignin peroxidases and versatile peroxidases, key elements of the enzymatic machineries secreted by white-rot fungi to degrade lignin, thus providing access to cellulose and hemicellulose in plant cell walls. A recent genomic analysis of 52 Agaricomycetes species revealed the existence of novel MnP subfamilies differing in the amino-acid residues that constitute the manganese oxidation site. Following this in silico analysis, a comprehensive structure-function study is needed to understand how these enzymes work and contribute to transform the lignin macromolecule. PubMed: 38824538DOI: 10.1186/s13068-024-02517-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.247 Å) |
Structure validation
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