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. Author manuscript; available in PMC: 2013 Sep 13.

Published in final edited form as: Nat Struct Mol Biol. 2013 May 26;20(7):900–907. doi: 10.1038/nsmb.2583

a, Schematic of Hsp70 domain structure. Structured subdomains are given color assignments and positions of key elements are identified.

b, Ribbon representation of the DnaK SBD- structure. Domain coloring is as in a. stands for loop. The Linker segment from a symmetry mate (in purple) binds to the polypeptide-binding site between and .

c, Superposition of SBDβ from the DnaK SBD- structure (colored as in b) with that of the WT SBD structure (orange; PDB 1DKZ). The peptide substrate NR in the WT SBD structure is colored in cyan.

d, Tryptophan-fluorescence emission spectra for assaying the ATP-induced allosteric coupling of DnaK.

Inline graphic — a, Schematic of Hsp70 domain structure. Structured subdomains are given color assignments and positions of key elements are identified.

b, Ribbon representation of the DnaK SBD- structure. Domain coloring is as in a. stands for loop. The Linker segment from a symmetry mate (in purple) binds to the polypeptide-binding site between and .

c, Superposition of SBDβ from the DnaK SBD- structure (colored as in b) with that of the WT SBD structure (orange; PDB 1DKZ). The peptide substrate NR in the WT SBD structure is colored in cyan.

d, Tryptophan-fluorescence emission spectra for assaying the ATP-induced allosteric coupling of DnaK.

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