6L27

X-ray crystal structure of the mutant green fluorescent protein

6L27 の概要

• エントリーDOI: 10.2210/pdb6l27/pdb
• 分子名称: Green fluorescent protein (2 entities in total)
• 機能のキーワード: gfp, mutant, recombinant, fluorescent protein
• 由来する生物種: Aequorea victoria (Jellyfish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25829.03

構造登録者

Adachi, M.,Shimizu, R.,Shibazaki, C.,Kagotani, Y.,Ostermann, A.,Schrader, T.E. (登録日: 2019-10-02, 公開日: 2020-04-01, 最終更新日: 2026-03-18)

主引用文献

Shibazaki, C.,Shimizu, R.,Kagotani, Y.,Ostermann, A.,Schrader, T.E.,Adachi, M.
Direct Observation of the Protonation States in the Mutant Green Fluorescent Protein.
J Phys Chem Lett, 11:492-496, 2020

PubMed Abstract: Neutron 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.

PubMed: 31880458
DOI: 10.1021/acs.jpclett.9b03252

実験手法

X-RAY DIFFRACTION (0.77 Å)