The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

@article{Xu1997TheCS,
  title={The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex},
  author={Zhaohui Xu and Arthur L. Horwich and Paul B. Sigler},
  journal={Nature},
  year={1997},
  volume={388},
  pages={741-750}
}
Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings of subunits stacked back to back. In Escherichia coli, asymmetric intermediates of GroEL are formed with the co-chaperonin GroES and nucleotides bound only to one of the seven-subunit rings (the cis ring) and not to the opposing ring (the trans ring). The structure of the GroEL–GroES–(ADP)7 complex reveals how large en bloc movements of the cis ring's intermediate and… 
GroEL/GroES: structure and function of a two-stroke folding machine.
TLDR
This work has shown that the asymmetric binding of ATP and cochaperonin GroES to GroEL triggers a major conformational change in the cis ring, creating an enlarged chamber into which the bound nonnative polypeptide is released and changes the lining of the cavity wall from hydrophobic to hydrophilic, conducive to folding into the native state.
GroEL Ring Separation and Exchange in the Chaperonin Reaction
Conformational Changes In GROEL Induced by a Protein Substrate
TLDR
The GroEL/GroES chaperonin system of E. coli facilitates nucleotide dependent folding of select proteins and provides flexibility for en bloc rearrangement associated with nucleotide and GroES binding.
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
TLDR
It is shown that for the folding of malate dehydrogenase and Rubisco there is also an absolute requirement for ATP in the cis ring, as ADP and AMP-PNP are unable to promote folding.
Chaperone Activity of a Chimeric GroEL Protein That Can Exist in a Single or Double Ring Form*
TLDR
It is demonstrated that the double ring structure of GroEL is likely to be required for its activity in vivo, while the single ring form of the GroEL chimera is able to chaperone the folding of a substrate that does not require GroES for its efficient folding.
Chaperonin complex with a newly folded protein encapsulated in the folding chamber
TLDR
Structures of gp23–chaperonin complexes are presented, showing both the initial captured state and the final, close-to-native state with gp23 encapsulated in the folding chamber, explaining why the GroEL–GroES complex is not able to fold gp23 and showing how the chaperon in structure distorts to enclose a large, physiological substrate protein.
Spontaneous conformational changes in the E. coli GroEL subunit from all-atom molecular dynamics simulations.
TLDR
A novel mechanism for inter-ring cooperativity in ATP binding inspired by the observation of spontaneous insertion of the side chain of Ala(480) into the empty nucleotide pocket is proposed.
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References

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TLDR
It is shown that for the folding of malate dehydrogenase and Rubisco there is also an absolute requirement for ATP in the cis ring, as ADP and AMP-PNP are unable to promote folding.
Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.
TLDR
The functional complex of GroEL and GroES is characterized by asymmetrical binding of GroES to one end of the GroEL cylinder and it is suggested that binding of the substrate protein occurs within the central cavity ofGroEL.
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TLDR
A mutational analysis is undertaken that relates the functional prop-erties of GroEL to its crystal structure and finds a highly conserved residue, Asp 87, positioned within a putative nucleotide-binding pocket in the top of the equatorial domain, is essential for ATP hydrolysis and polypeptide release.
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TLDR
A unifying model for chaperonin-facilitated protein folding based on successive rounds of binding and release, and partitioning between committed and kinetically trapped intermediates, is proposed.
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TLDR
The first direct visualization, by cryo-electron microscopy, of a non-native protein substrate (malate dehydrogenase) bound to the mobile, outer domains at one end of GroEL is reported.
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TLDR
The chaperonin GroEL is able to mediate protein folding in its central cavity by assuming its native conformation when the GroES cofactor caps one end of the GroEL cylinder, thereby discharging the unfolded polypeptide into an enclosed cage.
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TLDR
It is concluded that release of non-native forms from GroEL in vivo allows a kinetic partitioning among various chaperones and proteolytic components, which determines both the conformation and lifetime of a protein.
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits
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