The structure of mAG, a monomeric mutant of the green fluorescent protein Azami-Green, reveals the structural basis of its stable green emission

Acta Cryst. (2010). F66, 485-489 (doi.org/10.1107/S1744309110011127)

The unique QYG chromophore and the surrounding residues of mAG.

Azami-Green (AG) from the stony coral Galaxea fascicularis is a monomeric green-emitting fluorescent protein that is not a variant of Aequorea victoria green fluorescent protein (avGFP). The crystal structure of mAG has been determined at 2.2 Å resolution, which reveals the structural basis of the stable green emission of mAG. The conformation of the QYG chromophore, formed by Gln62-Tyr63-Gly64, is fixed by hydrogen bonds and van der Waals contacts with the surrounding residues. Particularly, His193, Arg66, and Thr69 contribute to the fixed conformation of the chromophore.