Journal of Biological Chemistry · 1998 · 63 citations · 31 references
Life SciencesBiochemistryMolecular BiologyMolecular BiophysicsProtein FoldingStructural BiologyChaperone-mediated FoldingMacromolecular AssemblyMolecular ChaperonesProtein DynamicsProtein Folding ThermodynamicsProtein StructureAtp-dependent Folding MechanismsChaperonin FunctionChaperonin-mediated FoldingEukaryotic ChaperonesNucleotide Binding DomainsProtein Conformational ChangesReversible Conformational ChangesStructural Biology Of Chaperones
The chaperonin-containing TCP-1 complex (CCT) is a heteromeric particle composed of eight different subunits arranged in two back-to-back 8-fold pseudo-symmetric rings. The structural and functional implications of nucleotide binding to the CCT complex was addressed by electron microscopy and image processing. Whereas ADP binding to CCT does not reveal major conformational differences when compared with nucleotide-free CCT, ATP binding induces large conformational changes in the apical and equatorial domains, shifting the latter domains up to 40 degrees (with respect to the inter-ring plane) compared with 10 degrees for nucleotide-free CCT or ADP-CCT. This equatorial ATP-induced shift has no counterpart in GroEL, its prokaryotic homologue, which suggests differences in the folding mechanism for CCT.
31
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
K. Braig, Zbyszek Otwinowski, Rashmi S. Hegde et al. · Nature · 1994 · 1.3K citations
A cytoplasmic chaperonin that catalyzes β-actin folding
Yijie Gao, J. O. Thomas, Robert L. Chow et al. · Cell · 1992 · 492 citations