ATP-dependent hexameric assembly of the heat shock protein Hsp101 involves multiple interaction domains and a functional C-proximal nucleotide-binding domain.

Abstract excerpt

Members of the Hsp100 family of heat stress proteins are present in species throughout the bacterial, plant, and fungal kingdoms. Most Hsp100 proteins are composed of five domains that include two nucleotide-binding domains required for their ATP-dependent oligomerization. Mutations within the first but not the second nucleotide-binding site disrupt self-assembly of bacterial Hsp100, whereas the reverse is true...

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