6G5Q
The structure of a carbohydrate active P450
Summary for 6G5Q
| Entry DOI | 10.2210/pdb6g5q/pdb |
| Descriptor | Cytochrome P450, 6-O-methyl-beta-D-galactopyranose, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
| Functional Keywords | p450, monooxygenase, carbohydrate-active enzyme, oxidoreductase |
| Biological source | Zobellia galactanivorans |
| Total number of polymer chains | 2 |
| Total formula weight | 92714.11 |
| Authors | Robb, C.S.,Hehemann, J.H. (deposition date: 2018-03-29, release date: 2018-11-21, Last modification date: 2024-01-17) |
| Primary citation | Robb, C.S.,Reisky, L.,Bornscheuer, U.T.,Hehemann, J.H. Specificity and mechanism of carbohydrate demethylation by cytochrome P450 monooxygenases. Biochem. J., 475:3875-3886, 2018 Cited by PubMed Abstract: Degradation of carbohydrates by bacteria represents a key step in energy metabolism that can be inhibited by methylated sugars. Removal of methyl groups, which is critical for further processing, poses a biocatalytic challenge because enzymes need to overcome a high energy barrier. Our structural and computational analysis revealed how a member of the cytochrome P450 family evolved to oxidize a carbohydrate ligand. Using structural biology, we ascertained the molecular determinants of substrate specificity and revealed a highly specialized active site complementary to the substrate chemistry. Invariance of the residues involved in substrate recognition across the subfamily suggests that they are critical for enzyme function and when mutated, the enzyme lost substrate recognition. The structure of a carbohydrate-active P450 adds mechanistic insight into monooxygenase action on a methylated monosaccharide and reveals the broad conservation of the active site machinery across the subfamily. PubMed: 30404923DOI: 10.1042/BCJ20180762 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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