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. Author manuscript; available in PMC: 2020 Jan 8.
Published in final edited form as: Nat Struct Mol Biol. 2019 Jul 8;26(8):671–678. doi: 10.1038/s41594-019-0257-3

Figure 5. An allosteric network mutated in HSP couples substrate binding to oligomerization and ATP hydrolysis.

Figure 5.

(a) Interaction network centered on R591. Residues colored plum and cyan for protomers B and C, respectively. Residues mutated in HSP are indicated with an asterix. All interactions depicted have a measured distance of less than 4 Å. (b) W749 makes van der Walls contacts with several hydrophobic residues mutated in HSP and connects pore loop 3 to the C-terminal helix α11 involved in oligomerization. Residues are colored purple and cyan for protomers C and D, respectively. Residues mutated in HSP are indicated with an asterix. All interactions depicted have a measured distance of less than 4 Å.