Structural highlights
Function[GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. Publication Abstract from PubMedNeutron crystallography has been used to elucidate the protonation states for the enhanced green fluorescent protein, which has revolutionized imaging technologies. The structure has a deprotonated hydroxyl group in the fluorescent chromophore. Also, the protonation states of His148 and Thr203, as well as the orientation of a critical water molecule in direct contact with the chromophore, could be determined. The results demonstrate that the deprotonated hydroxyl group in the chromophore and the nitrogen atom ND1 in His148 are charged negatively and positively, respectively, forming an ion pair. The position of the two deuterium atoms in the critical water molecule appears to be displaced slightly toward the acceptor oxygen atoms according to their omit maps. This displacement implies the formation of an intriguing electrostatic potential realized inside of the protein. Our findings provide new insights into future protein design strategies along with developments in quantum chemical calculations. Direct Observation of the Protonation States in the Mutant Green Fluorescent Protein.,Shibazaki C, Shimizu R, Kagotani Y, Ostermann A, Schrader TE, Adachi M J Phys Chem Lett. 2020 Jan 16;11(2):492-496. doi: 10.1021/acs.jpclett.9b03252., Epub 2020 Jan 6. PMID:31880458[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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