The mechanism of folding robustness revealed by the crystal structure of extra-superfolder GFP
The mechanism of folding robustness revealed by the crystal structure of extra-superfolder GFP
复制标题
DOI：
10.1002/1873-3468.12534
复制
发表时间：
2017-01-01
期刊：
影响因子：
3.5
通讯作者：
Park, Hyun Ho
中科院分区：
文献类型：
--
作者：
Choi, Jae Young;Jang, Tae-Ho;Park, Hyun Ho
绿色荧光蛋白（GFP）的稳定性有时对该蛋白的实际应用至关重要。随机诱变和靶向诱变已被用于创建更好折叠的GFP变体，包括最近报道的超文件夹GFP。我们的目的是确定超折叠GFP的晶体结构，它比GFP和超折叠GFP具有更强的折叠性和稳定性。结构和基于结构的突变分析显示，一些产生超夹GFP的突变（F46L、E126K、N149K和S208L）通过稳定各种非共价键的超夹GFP来促进折叠稳健性。
Stability of green fluorescent protein (GFP) is sometimes important for a proper practical application of this protein. Random mutagenesis and targeted mutagenesis have been used to create better-folded variants of GFP, including recently reported extra-superfolder GFP. Our aim was to determine the crystal structure of extra-superfolder GFP, which is more robustly folded and stable than GFP and superfolder GFP. The structural and structure-based mutagenesis analyses revealed that some of the mutations that created extra-superfolder GFP (F46L, E126K, N149K, and S208L) contribute to folding robustness by stabilizing extra-superfolder GFP with various noncovalent bonds.