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Literature summary for 3.6.4.10 extracted from

  • Nagy, M.; Akoev, V.; Zolkiewski, M.
    Domain stability in the AAA+ ATPase ClpB from Escherichia coli (2006), Arch. Biochem. Biophys., 453, 63-69.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
F105W/W462F/W543F mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity Escherichia coli
F276W/W462F/W543F mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity Escherichia coli
F603W/W462F/W543F mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity Escherichia coli
W462F mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity Escherichia coli
W462F/W543F mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity Escherichia coli
W543F mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity Escherichia coli
Y251W/W462F/W543F mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity Escherichia coli
Y812/W462F/W543F mutant constructed for thermodynamic analysis. Similar to wild-type, variant efficiently forms oligomers at high protein concentration, and shows ATPase activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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 isoform ClpB
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Subunits

Subunits Comment Organism
heptamer ClpB is monomeric in high ionic-strength buffers of 0.2-0.3 M KCl, whereas heptameric ClpB predominates at low ionic strength. The small domain of the C-terminal AAA+ module and the coiled-coil domain are destabilized in the oligomeric form Escherichia coli
monomer ClpB is monomeric in high ionic-strength buffers of 0.2-0.3 M KCl, whereas heptameric ClpB predominates at low ionic strength. The small domain of the C-terminal AAA+ module and the coiled-coil domain are destabilized in the oligomeric form Escherichia coli