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6G5O

The structure of a carbohydrate active P450

Summary for 6G5O
Entry DOI10.2210/pdb6g5o/pdb
DescriptorCytochrome P450, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
Functional Keywordsp450, monooxygenase, carbohydrate-active enzyme, oxidoreductase
Biological sourceZobellia galactanivorans
Total number of polymer chains2
Total formula weight92233.65
Authors
Robb, C.S.,Hehemann, J.H. (deposition date: 2018-03-29, release date: 2018-11-21, Last modification date: 2024-01-17)
Primary citationRobb, 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: 30404923
DOI: 10.1042/BCJ20180762
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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