Literature summary for 3.6.4.10 extracted from

Swain, J.F.; Schulz, E.G.; Gierasch, L.M.
Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states (2006), J. Biol. Chem., 281, 1605-1611.

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Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
additional information	-	the isolated beta-subdomain,a DnaK substrate-binding domain fragment retaining a portion of the alpha-helical subdomain but harboring mutations that abrogate self-binding is well folded and stable in the empty state and binds peptides with high affinity. When this stable substrate-binding domain and the native ATPase domain are linked in a two-domain construct, the protein is allosterically functional. The two domains of the two-domain construct do not interact, even in the presence of peptide. Nucleotide is necessary to establish allosteric signaling between the domains	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Synonyms

Synonyms	Comment	Organism
Hsp70	-	Escherichia coli

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Release 2023.1 (January 2023)