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. 2009 Nov 4;19(1):57–65. doi: 10.1002/pro.282

Figure 1.

Figure 1

Distinct conformational states of the Hsp90 molecular chaperone. Previous crystallography, electron microscopy, and small angle x-ray scattering (SAXS) measurements have determined a multi-state conformational equilibrium for the Hsp90 homolog from E. coli, HtpG.20–22 The relative population of these conformations can be determined from SAXS measurements and structure-based fitting. The ATP state was modeled from a crystal structure of a yeast Hsp90 homolog.19,20 The closed state is similar to a crystal structure of the Hsp90 homolog from the ER, Grp94, and has been referred to as a Grp94-like state.