An important development in the field of carbohydrate-active enzymes is the identification of the lytic polysaccharide monooxygenases (LPMOs). These proteins are copper-dependent metalloenzymes that cleave the β-1,4 glycosidic bonds of polysaccharides by an oxidative mechanism. The conserved active site property that unifies the three LPMO families is the copper binding site. One copper atom is coordinated by three nitrogen ligands provided by two histidine imidazoles and the N-terminal amino group in a T-shaped histidine brace arrangement. Here you can see a crystal structure of the chitin-active AA10 LPMO (GbpA) from Vibrio campbellii (PDB code: 8GUM)

#molecularart ... #immolecular ... #vibrio ... #chitin ... #carbohydrate... #copper... #xray

Structure rendered with @proteinimaging and depicted with @corelphotopaint