Proton pathways in green fluorescence protein
Proton pathways in green fluorescence protein
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DOI:
10.1529/biophysj.104.055541
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发表时间:
2005-04-01
影响因子:
3.4
通讯作者:
Agmon, N
中科院分区:
文献类型:
--
作者:
Agmon, N
Proton pathways in green fluorescent protein (GFP) are more extended than previously reported. In the x-ray data of wild-type GFP, a two-step exit pathway exists from the active site to the protein surface, controlled by a threonine switch. A proton entry pathway begins at a glutamate-lysine cluster around Glu-5, and extends all the way to the buried Glu-222 near the active site. This structural evidence suggests that GFP may function as a portable light-driven proton-pump, with proton emitted in the excited state through the switchable exit pathway, and replenished from Glu-222 and the Glu-5 entry pathway in the ground state.