Exploring the Functional Complementation between Grp94 and Hsp90
Fig 7
The M1 domain of Grp94 and Hsp90 differ in their surface residues.
A) Alignment of the M1 lobe of the M domains of Grp94, yeast Hsp90, and human Hsp90. Grp94 residues highlighted in yellow differ from the yeast and human Hsp90 consensus. Purple boxes indicate residues shown to be mutagenically sensitive in yeast Hsp90 for client maturation. Green boxes indicate residues of human Hsp90 that interact with Cdc37 in the cryo-EM structure of Cdk4-Cdc37-Hsp90 (PDB code 5fwl). Asterisks and numbers (Grp94 numbering) highlight Cdc37-interacting residues that differ between Hsp90 and Grp94. B) Mapping the unique residues onto the structure of the Grp94 dimer. PDB code 2o1v was used. Residues highlighted in yellow in A) are shown as sticks or spheres on the on protomers A and B, respectively. Green colored residues correspond to residues highlighted with asterisks in panel A.
