Gauging of the PhoE Channel by a Single Freely Diffusing Proton

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Gauging of the PhoE Channel by a Single Freely Diffusing Proton Sharron Bransburg-Zabary, Esther Nachliel, Menachem Gutman  Biophysical Journal  Volume 83, Issue 6, Pages 2987-3000 (December 2002) DOI: 10.1016/S0006-3495(02)75305-8 Copyright © 2002 The Biophysical Society Terms and Conditions

Figure 1 A GRASP presentation of the surface electrostatic potential of PhoE (left panel) and of the protein-pyranine complex (right panel). The pyranine, colored in yellow, is located in its most probable location. The upper panels (left and right) depict the electrostatic potential on the protein's surface looking down the channel from the extracellular side. The other panels depict the channel when cut in half through the YZ plane, as marked by the line in the top image. The color scale of the potentials is given at the bottom of the figure. Biophysical Journal 2002 83, 2987-3000DOI: (10.1016/S0006-3495(02)75305-8) Copyright © 2002 The Biophysical Society Terms and Conditions

Figure 2 A schematic energy profile of successive slices perpendicular to the z axis. (A) The potential of the i slice is lower than that of the next one. As a result, as the proton advances to slice i+1 it will scan all surface points whose potential is lower than the minimum of the i+1 slice. The scanned area is marked by hatching. (B) The propagation of the proton along the z axis is downhill. In that case the area scanned by the proton is bound in the range Emin to Emin+kBT. Biophysical Journal 2002 83, 2987-3000DOI: (10.1016/S0006-3495(02)75305-8) Copyright © 2002 The Biophysical Society Terms and Conditions

Figure 3 The most probable location of pyranine in the PhoE channel as seen from the periplasmic side of the channel. The protein is schematically represented by the yellow plats for the β-sheets, green lines for random coils, and a red cylinder for the α helix. The pyranine is given in atomic detail. The charged residues located within 15 E from the pyranine molecule (blue for basic and red for acidic residues) are presented in ball-and-stick format. Biophysical Journal 2002 83, 2987-3000DOI: (10.1016/S0006-3495(02)75305-8) Copyright © 2002 The Biophysical Society Terms and Conditions

Figure 4 The maps of the electrostatic potential inside the channel as calculated for the PhoE-pyranine complex. Frames (A) and (B) depict the potentials in the extracellular and periplasmic sections of the channel, respectively. Each image maps the potential in a 0.33Å thick slice. The slices are 2Å apart along axis z of the channel. The slice on the upper left corners (Z=−8 and Z=5) are the closest ones to the pyranine molecule and serve as the sites where the proton is initially released. The protein is represented by the dotted region. The red dots at Z=5 and Z=−8 represent the Na+ ions that were inserted in the potential traps. The potential scale is given by the color code and the units are kBT. Biophysical Journal 2002 83, 2987-3000DOI: (10.1016/S0006-3495(02)75305-8) Copyright © 2002 The Biophysical Society Terms and Conditions

Figure 4 The maps of the electrostatic potential inside the channel as calculated for the PhoE-pyranine complex. Frames (A) and (B) depict the potentials in the extracellular and periplasmic sections of the channel, respectively. Each image maps the potential in a 0.33Å thick slice. The slices are 2Å apart along axis z of the channel. The slice on the upper left corners (Z=−8 and Z=5) are the closest ones to the pyranine molecule and serve as the sites where the proton is initially released. The protein is represented by the dotted region. The red dots at Z=5 and Z=−8 represent the Na+ ions that were inserted in the potential traps. The potential scale is given by the color code and the units are kBT. Biophysical Journal 2002 83, 2987-3000DOI: (10.1016/S0006-3495(02)75305-8) Copyright © 2002 The Biophysical Society Terms and Conditions

Figure 5 The most probable trajectories for proton propagation inside the PhoE channel. The protein is represented by the backbone structure of a single monomer. The pyranine is presented, in a space-filled model, at its most probable location at the center of the protein. The most probable trajectory is composed of two routes, the extracellular (purple) and the periplasmic (orange), by R=1Å spheres. The lower section of the figure depicts the electrostatic potentials along the two routes as calculated by the DelPhi program. The lowest potential, at Z=−8, is defined as zero. Biophysical Journal 2002 83, 2987-3000DOI: (10.1016/S0006-3495(02)75305-8) Copyright © 2002 The Biophysical Society Terms and Conditions

Figure 6 Reconstruction of the measured fluorescence decay dynamics of the excited pyranine inside the PhoE channel. The main frame depicts the experimental signal and the reconstruction dynamics on a linear scale, to emphasize the quality of the fit in the short time range. The inset presents the data on a logarithmic ordinate, demonstrating that the fit is valid down to 0.1% of the initial amplitude, 20ns after the initiation of the proton dissociation. The lower frame presents the residue (measured signal minus calculated value) expanded fourfold. The simulation was carried out with the parameters listed in Table 2. Biophysical Journal 2002 83, 2987-3000DOI: (10.1016/S0006-3495(02)75305-8) Copyright © 2002 The Biophysical Society Terms and Conditions

Figure 7 The effect of the adjustable parameters on the reconstructed dynamics. In each frame there are three curves that were calculated with the parameters given in Table 2, except for a single parameter that was set to be either 30% higher or lower than the best-fit value. In (A) the rate constant of proton dissociation (κf) was varied. To demonstrate that the deviation from the experimental curve is detected right from the beginning of the reaction, the dynamics are presented in an expanded time scale. Frame (B) demonstrates how the proton recombination rate (κr) affects the dynamics. Please notice that most initial dynamics are hardly affected by κr. Frame (C) demonstrates how the proton interaction with the carboxylates residues in the channel affects the fluorescence relaxation dynamics. Biophysical Journal 2002 83, 2987-3000DOI: (10.1016/S0006-3495(02)75305-8) Copyright © 2002 The Biophysical Society Terms and Conditions