Fig. 2

Schematic of co-chaperones Aha1p and Hch1p and their interaction with Hsp90. a Hch1p corresponds to the N terminal domain of Aha1p which is connected to the C domain by a flexible linker. b Hch1p and the Aha1p N domain interact with the middle domain of Hsp90. The Aha1p C domain interacts with the N terminal domains of Hsp90. c A model of the complex between the Hsp90 middle domain (light green) and the Aha1p N domain (cyan) (1USV¹⁹). The RKxK motif is colored in orange and residues Trp11 and Val12 (magenta) indicate where the N terminal NxNNWHW motif would be present (it is unstructured in 1USV). d The structure shown in c is aligned to the full length, closed Hsp90 dimer structure (2CG9³³) with the two Sba1p subunits masked. ATP is depicted in blue wireframe. The NxNNWHW motif is predicted to be oriented towards the Hsp90 N domains