E. coli GroS, recombinant protein from E. coli
Escherichia coli groS (NP_418566) recombinant protein expressed inEscherichia coli .
In 25 mM Tris-HCl, 100mM NaCl, pH 7.5 (5 mM DTT, 10% glycerol)
2-8°C short term, -20°C long term
GroS binds and regulates rpoH. [More information is available at EcoGene: EG10600]. The Escherichia coli chaperone protein GroEL (Hsp60) and its regulator GroES are necessary for the proper folding of certain proteins , . [More information is available at EcoCyc: EG10600].
GroEL and GroES are E.coli chaperones, which are homologs of the mitochondrial chaperones Hsp60 and Hsp10 respectively. GroEL is a double toriodal assembly of 14 identical subunits which form two heptameric rings stacked back-to-back, with a cavity at each end. GroEL and its co-chaperonin GroES facilitate protein folding in an ATP-dependent mechanism. Binding of substrate protein, in addition to binding of ATP, induces a conformational change that allows association of this binary complex with a separate lid structure, GroES.