6Y0R

Chitooligosaccharide oxidase

This is a non-PDB format compatible entry.

Summary for 6Y0R

• Entry DOI: 10.2210/pdb6y0r/pdb
• Descriptor: Chitooligosaccharide oxidase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: flavin-dependent, oxidase, oligosaccharides, covalent fad, oxidoreductase
• Biological source: Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084)
• Total number of polymer chains: 1
• Total formula weight: 53453.89

Authors

Savino, S.,Fraaije, M.W. (deposition date: 2020-02-10, release date: 2020-06-03, Last modification date: 2024-11-13)

Primary citation

Savino, S.,Jensen, S.,Terwisscha van Scheltinga, A.,Fraaije, M.W.
Analysis of the structure and substrate scope of chitooligosaccharide oxidase reveals high affinity for C2-modified glucosamines.
Febs Lett., 594:2819-2828, 2020

PubMed Abstract: Chitooligosaccharide oxidase (ChitO) is a fungal carbohydrate oxidase containing a bicovalently bound FAD cofactor. The enzyme is known to catalyse the oxidation of chitooligosaccharides, oligomers of N-acetylated glucosamines derived from chitin degradation. In this study, the unique substrate acceptance was explored by testing a range of N-acetyl-d-glucosamine derivatives, revealing that ChitO preferentially accepts carbohydrates with a hydrophobic group attached to C2. The enzyme also accepts streptozotocin, a natural product used to treat tumours. Elucidation of the crystal structure provides an explanation for the high affinity towards C2-decorated glucosamines: the active site has a secondary binding pocket that accommodates groups attached at C2. Docking simulations are fully in line with the observed substrate preference. This work expands the knowledge on this versatile enzyme.

PubMed: 32491191
DOI: 10.1002/1873-3468.13854

Experimental method

X-RAY DIFFRACTION (1.611 Å)