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Literature summary for 3.6.4.10 extracted from

  • General, I.J.; Liu, Y.; Blackburn, M.E.; Mao, W.; Gierasch, L.M.; Bahar, I.
    ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones (2014), PLoS Comput. Biol., 10, e1003624.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.10

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Escherichia coli
-
 ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Escherichia coli ADP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
heat shock protein 70
-
 Escherichia coli
Hsp70
-
 Escherichia coli

General Information

General Information Comment Organism
additional information identification of a network of conserved interactions in subdomain IA of the nucleotide-binding domain, which plays a key (effector) role in propagating signals between the ATP-binding and substrate-binding sites. Subdomain IIA, on the other hand, appears to adapt to J-domain co-chaperone binding by virtue of a broadly distributed cluster of co-evolving residues on the recognition surface. L177 plays a key role in conveying signals from the linker and DnaJ-binding site to the ATP-binding site. V389 exhibits a strong co-variance with L177, a hydrophobic residue at the linker-binding pocket. L177, in turn, is highly correlated with I373, another hydrophobic residue in the vicinity of the linker-binding pocket. Nucleotide-binding domain subdomain IA, and in particular a number of highly conserved (V139, D148, K155, R167, N170, E171) or co-evolving (R159, L177) residues therein, serve as mediators of communication between the substrate- and nucleotide-binding sites of the respective SBD and NBD, in addition to their involvement in relaying signals from the DnaJ-binding site to the ATP-binding site. Residues involved in co-chaperone recognition and their coupling to the NBD-SBD interfacial region, overview Escherichia coli
physiological function the Hsp70 family of molecular chaperones assists in protein folding, degradation, assembly/disassembly of some complexes, and intracellular trafficking. These activities in the cell are accomplished by coupled conformational switches/signals between their nucleotide-binding and substrate-binding domains (NBD and SBD), assisted by cognate co-chaperones Escherichia coli