Proton pathways in green fluorescence protein

Noam Agmon*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

98 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)2452-2461
Number of pages10
JournalBiophysical Journal
Volume88
Issue number4
DOIs
StatePublished - Apr 2005

Fingerprint

Dive into the research topics of 'Proton pathways in green fluorescence protein'. Together they form a unique fingerprint.

Cite this