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. 2019 Jun 12;10:2574. doi: 10.1038/s41467-019-10463-y

Fig. 4.

Fig. 4

Y313E-induced conformational changes probed by methyl-TROSY NMR. Selected regions from the overlay of the 1H-13C-HMQC spectra of wild-type (black) and Hsp90-Y313E (red), showing signals that experience changes in chemical shifts and significant line broadening. The bottom panel includes an overlay of wild-type Hsp90 in the AMPPNP bound state (green) for I26 and I110 that undergo large chemical shift changes upon nucleotide addition due to Hsp90-N/N dimerization (see Supplementary Fig. 4). The Ile residues that experience significant chemical shift changes after phosphomimetic mutation mapped on the structure of Hsp90 in the closed state. One subunit is shown in gray, while in the other subunit N-, M- and C-domain of Hsp90 are colored blue, green, and orange, respectively. The site of the phosphomimetic mutation is shown in pink. Source data for this figure are provided as a Source Data File