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
the biologically active form of bacterial ClpB is a cylinder-shaped homohexamer. The self-association of ClpB into hexamers is induced by nucleotide binding
each monomer contains four domains, an N-terminal domain, two nucleotide-binding domains (NBD1 and NBD2), and a middle (M) domain. The M domain, which is specific for ClpB and its homologues, is inserted into the NBD1, folds as a coiled-coil structure built up by four helices. ATP binding to ClpB stabilizes the protein hexamer and ADP dissociates it
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
1 * 36000-66000, recombinant enzyme, monomeric and monodisperse mortalin, analytical ultracentrifugation and crystal structure analysis, mortalin has an elongated shape in solution, modeling, overview
the C-terminal alpha-helical subdomain is involved in higher order associations, while the substrate binding domain is possibly involved in dimerisation
unlike Hsp100s, Hsp70-type chaperones do not oligomerize. They transiently associate with exposed hydrophobic segments of client proteins via a carboxy-terminal substrate binding domain (SBD), thereby preventing aggregation and promoting proper folding
unlike Hsp100s, Hsp70-type chaperones do not oligomerize. They transiently associate with exposed hydrophobic segments of client proteins via a carboxy-terminal substrate binding domain (SBD), thereby preventing aggregation and promoting proper folding
dissection of the BiP molecular network. Protein Grp170 is the major nucleotide exchange factor for BiP, and endoplasmic reticulum-resident J-domain protein 1 plus endoplasmic reticulum-resident J-domain protein 2/Sec63 are prime candidates for cochaperones of BiP in protein transport in the pancreas
although monomeric Hsp70 is very sensitive to hydrostatic pressure, the protein does not return to its native state after removal of the pressure but instead forms oligomeric species that lose chaperone activity but retain ATPase activity, overview
all Hsp70 molecules possess a conserved architecture that consists of a 44 kDa N-terminal adenine nucleotide-binding domain (NBD), an 18 kDa substrate-binding domain (SBD), and a 10 kDa C-terminal domain (CTD)
all Hsp70 molecules possess a conserved architecture that consists of a 44 kDa N-terminal adenine nucleotide-binding domain (NBD), an 18 kDa substrate-binding domain (SBD), and a 10 kDa C-terminal domain (CTD)
unlike Hsp100s, Hsp70-type chaperones do not oligomerize. They transiently associate with exposed hydrophobic segments of client proteins via a carboxy-terminal substrate binding domain (SBD), thereby preventing aggregation and promoting proper folding
unlike Hsp100s, Hsp70-type chaperones do not oligomerize. They transiently associate with exposed hydrophobic segments of client proteins via a carboxy-terminal substrate binding domain (SBD), thereby preventing aggregation and promoting proper folding
unlike Hsp100s, Hsp70-type chaperones do not oligomerize. They transiently associate with exposed hydrophobic segments of client proteins via a carboxy-terminal substrate binding domain (SBD), thereby preventing aggregation and promoting proper folding
unlike Hsp100s, Hsp70-type chaperones do not oligomerize. They transiently associate with exposed hydrophobic segments of client proteins via a carboxy-terminal substrate binding domain (SBD), thereby preventing aggregation and promoting proper folding
primary enzyme structures and temperature-dependent oligomeric structural changes of Hsp14.0, Hsp14.0 exists as a spherical 24-meric oligomer, while Hsp19.7 of Sulfolobus tokodaii forms a filamentous structure in vivo consisting of spherical particles. Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, overview
primary enzyme structures and temperature-dependent oligomeric structural changes of Hsp14.0, Hsp14.0 exists as a spherical 24-meric oligomer, while Hsp19.7 of Sulfolobus tokodaii forms a filamentous structure in vivo consisting of spherical particles. Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, overview