Extended Data Fig. 7: The cryo-EM density and atomic model of GRHelix 1 motif interacting with Hsp90 and HopDP2.
From: Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism
a, The focused map of the Hsp90ABCTD:Hsp70CSBD-β:HopDP2:GRHelix 1 (top) and the atomic model shown in ribbon representation (bottom). b, The top view of the reconstruction and model shown in a. c, The density (mesh) for the GRHelix 1 motif (residues 528-551) gripped by Hsp90 and HopDP2. d, The atomic interactions of the GRHelix 1 motif with Hsp90 and HopDP2 corresponding to b, cyan box in bottom). Residues in contact with the GR motif are shown in stick representation. The types of molecular interaction Hsp90 and HopDP2 provide are indicated at the top; H and P denote hydrophobic and polar interactions, respectively. e, The 7Å low-pass filtered cryo-EM map shows that the lumen density (yellow shade) of GR connects to the globular part of GR on the other side of Hsp90. f, Docking of the GRLBD to the 10Å low-pass filtered map shows that the low-resolution GR density can fit the rest of the GRLBD. g, The low-pass filtered map shows that W320 and F349 (arrows) of Hsp90A in the loading complex are in contact with GRLBD.
