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Visualizing Proton Antenna in a High-Resolution Green Fluorescent Protein Structure

Summary: Visualizing Proton Antenna in a High-Resolution Green
Fluorescent Protein Structure
Ai Shinobu,
Gottfried J. Palm,*,
Abraham J. Schierbeek,,
and Noam Agmon*,
The Fritz Haber Research Center, Institute of Chemistry, The Hebrew UniVersity of Jerusalem,
Jerusalem 91904, Israel, Institute for Chemistry and Biochemistry,
Ernst-Moritz-Arndt-UniVersity, 17489 Greifswald, Germany, Bruker AXS B.V., Oostsingel 209,
Delft NL-2612 HL, The Netherlands, and Rigaku Europe, Unit B6, Chaucer Business Park,
Watery Lane, Kemsing, SeVenoaks, Kent TN15 6QY, England
Received February 14, 2010; E-mail: palm@uni-greifswald.de; agmon@fh.huji.ac.il
Abstract: "Proton-collecting antenna" are conjectured to consist of several carboxylates within hydrogen-
bond (HB) networks on the surface of proteins, which funnel protons to the orifice of an internal proton
wire leading to the protein's active site. Yet such constructions were never directly visualized. Here we
report an X-ray structure of green fluorescent protein (GFP) of the highest resolution to date (0.9 ). It
allows the identification of some pivotal hydrogen atoms pertinent to uncertainties concerning the protonation
state of the chromophore. Applying a computer algorithm for mapping proton wires in proteins reveals the
previously observed "active site wire" connecting Glu222 with the surface carboxylate Glu5. In addition, it
is now possible to identify what appears to be a proton-collecting apparatus of GFP. It consists of a negative


Source: Agmon, Noam - Institute of Chemistry, Hebrew University of Jerusalem


Collections: Chemistry