原创力文档crystal structure of enhanced green fluorescent protein to 1.35 ？ resolution reveals alternative conformations for glu222增强型绿色荧光蛋白的晶体结构1.35 分辨率显示替代glu222构象.pdfVIP
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crystal structure of enhanced green fluorescent protein to 1.35 ？ resolution reveals alternative conformations for glu222增强型绿色荧光蛋白的晶体结构1.35 分辨率显示替代glu222构象
Crystal Structure of Enhanced Green Fluorescent Protein
˚
to 1.35 A Resolution Reveals Alternative Conformations
for Glu222
1¤ 2 1
James A. J. Arpino , Pierre J. Rizkallah , D. Dafydd Jones *
1 School of Biosciences, Cardiff University, Cardiff, United Kingdom, 2 School of Medicine, Cardiff University, Cardiff, United Kingdom
Abstract
Enhanced Green Fluorescent Protein (EGFP) is one of the most widely used engineered variants of the original wild-type
˚
Green Fluorescent Protein. Here, we report the high resolution (1.35 A) structure of EGFP crystallised in its untagged
sequence form that reveals the combined impact of the F64L and S65T, that give rise to improved folding and spectral
characteristics. The overall structure of EGFP is very similar to wt GFP, forming the classical b-barrel fold with the
chromophore containing helix running through the core of the structure. Replacement of Phe64 with Leu in EGFP results in
subtle rearrangement of hydrophobic core packing close to the chromophore including the reduction in surface exposure
of two hydrophobic residues. Replacement of Ser65 with Thr has a significant impact on the local hydrogen bond network
in the vicinity of the chromophore. Detailed analysis of electron density reveals that several residues close to the
chromophore occupy at least two distinct conformations. This includes Glu222 that defines the charged state on the
chromophore, with the two conformations having slightly different effects on the hydrogen bond network surrounding the
chromophore. Hence, the reported high-resolution structure of EGFP has provided a l
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