4TVF
OxyB from Actinoplanes teichomyceticus
Summary for 4TVF
| Entry DOI | 10.2210/pdb4tvf/pdb |
| Descriptor | OxyB, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | cytochrome p450 phenolic coupling enzyme teicoplanin biosynthesis, oxidoreductase |
| Biological source | Actinoplanes teichomyceticus |
| Total number of polymer chains | 1 |
| Total formula weight | 48270.77 |
| Authors | Haslinger, K.,Cryle, M.J. (deposition date: 2014-06-26, release date: 2014-11-12, Last modification date: 2023-12-20) |
| Primary citation | Haslinger, K.,Maximowitsch, E.,Brieke, C.,Koch, A.,Cryle, M.J. Cytochrome P450 OxyBtei Catalyzes the First Phenolic Coupling Step in Teicoplanin Biosynthesis. Chembiochem, 15:2719-2728, 2014 Cited by PubMed Abstract: Bacterial cytochrome P450s form a remarkable clade of the P450 superfamily of oxidative hemoproteins, and are often involved in the biosynthesis of complex natural products. Those in a subgroup known as "Oxy enzymes" play a crucial role in the biosynthesis of glycopeptide antibiotics, including vancomycin and teicoplanin. The Oxy enzymes catalyze crosslinking of aromatic residues in the non-ribosomal antibiotic precursor peptide while it remains bound to the non-ribosomal peptide synthetase (NRPS); this crosslinking secures the three-dimensional structure of the glycopeptide, crucial for antibiotic activity. We have characterized OxyBtei , the first of the Oxy enzymes in teicoplanin biosynthesis. Our results reveal that OxyBtei possesses a structure similar to those of other Oxy proteins and is active in crosslinking NRPS-bound peptide substrates. However, OxyBtei displays a significantly altered activity spectrum against peptide substrates compared to its well-studied vancomycin homologue. PubMed: 25358800DOI: 10.1002/cbic.201402441 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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