Protein Mobility of the Functional Regions in the HtpG Structures.

<p>The protein mobility of the HtpG structures : (<b>A</b>) extended apo-HtpG solution structure; (<b>B</b>) V-shaped apo-HtpG; and (<b>C</b>) ADP-bound, compact HtpG form. For comparison with the experimental data, the following protein segments monitored in HX-MS experiments <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0037605#pone.0037605-Graf1" target="_blank">[70]</a> were mapped onto the HtpG structures: residues 121–127 (NTD), 192–206 (NTD), 319–334 (M-domain), and 336–359 (M-domain). The Hsp90 structures are depicted in ribbons overlayed with the surface representation at the 50% transparency according to PyMOL. A surface-based representation colored (blue-to-red) according to the protein residue motilities (from more rigid-blue regions to more flexible-red regions). The functional protein segments are shown as spheres with the coloration reflecting changes in their mobility among different structural forms of HtpG.