4CUO
Banyan peroxidase with glycosylation
Summary for 4CUO
| Entry DOI | 10.2210/pdb4cuo/pdb |
| Descriptor | BANYAN PEROXIDASE, SULFATE ION, CARBONATE ION, ... (12 entities in total) |
| Functional Keywords | oxidoreductase, class iii, glycosylation, succinimide |
| Biological source | FICUS BENGHALENSIS (BANYAN TREE) |
| Total number of polymer chains | 1 |
| Total formula weight | 37699.90 |
| Authors | Palm, G.J.,Sharma, A.,Hinrichs, W. (deposition date: 2014-03-20, release date: 2014-07-23, Last modification date: 2024-11-20) |
| Primary citation | Palm, G.J.,Sharma, A.,Kumari, M.,Panjikar, S.,Albrecht, D.,Jagannadham, M.V.,Hinrichs, W. Post-Translational Modification and Extended Glycosylation Pattern of a Plant Latex Peroxidase of Native Source Characterized by X-Ray Crystallography. FEBS J., 281:4319-, 2014 Cited by PubMed Abstract: The crystal structure of banyan peroxidase purified from the latex of Ficus benghalensis has been solved at 1.67 Å resolution by single-wavelength anomalous diffraction phasing. The refined structure includes 306 amino acid residues, a heme and two calcium ions. The protein belongs to class III peroxidases and is the first one from plant latex. Extensive glycosylation was observed with N-linked glycans attached to seven asparagine residues. The enzyme is stable with respect to a wide pH range, temperature, chemical denaturants and organic solvents, probably as a result of its high glycosylation. An unexpected post-translational modification of Asp290 was identified as succinimide moiety. Kinetic parameters of banyan peroxidase have been determined using various hydrogen donor substrates and hydrogen peroxide. PubMed: 24980207DOI: 10.1111/FEBS.12900 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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