4tvf | pdb_00004tvf

OxyB from Actinoplanes teichomyceticus

spinqualitylabelsall models 4tvf, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tvf is a 1 chain structure with sequence from "actinoplanes_teichomyceticus"_parenti_et_al._1978 "actinoplanes teichomyceticus" parenti et al. 1978. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM Gene: tcp20 ("Actinoplanes teichomyceticus" Parenti et al. 1978) Activity: Unspecific monooxygenase, with EC number 1.14.14.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Cytochrome P450 OxyB Catalyzes the First Phenolic Coupling Step in Teicoplanin Biosynthesis.,Haslinger K, Maximowitsch E, Brieke C, Koch A, Cryle MJ Chembiochem. 2014 Oct 30. doi: 10.1002/cbic.201402441. PMID:25358800 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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