The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

@article{Braig1994TheCS,
  title={The crystal structure of the bacterial chaperonln GroEL at 2.8 {\AA}},
  author={Kerstin Braig and Zbyszek Otwinowski and Rashmi S Hegde and David C. Boisvert and Andrzej J Joachimiak and Arthur L. Horwich and Paul B. Sigler},
  journal={Nature},
  year={1994},
  volume={371},
  pages={578-586}
}
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 consist of three domains: a large equatorial domain that forms the foundation of the assembly at its waist and holds the rings together; a large loosely structured apical domain that forms the ends of the cylinder; and a small slender intermediate domain that connects the two, creating side windows… Expand
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
TLDR
The 'mobile loop' segment, previously identified as a GroEL binding determinant, is disordered in the crystal structure in six subunits; the single well-ordered copy extends from the bottom outer rim of the GroES dome, suggesting that the cavity within the dome is continuous with the polypeptide binding chamber of GroEL in the chaperonin complex. Expand
The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
TLDR
The crystal structure of GroEL with ATPγS bound to each subunit shows that ATP binds to a novel pocket, whose primary sequence is highly conserved among chaperonins. Expand
The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
TLDR
The structure of the GroEL–GroES–(ADP)7 complex reveals how large en bloc movements of the cis ring's intermediate and apical domains enable bound GroES to stabilize a folding chamber with ADP confined to the cisRing, suggesting a model for an ATP-driven folding cycle that requires a double toroid. Expand
Structural aspects of GroEL function.
  • A. Horovitz
  • Biology, Medicine
  • Current opinion in structural biology
  • 1998
TLDR
The recently solved crystal structure of the GroES.(ADP)7 complex shows that the lining of the cavity in the polypeptide acceptor state is hydrophobic, whereas in the protein-release state it becomes hydrophilic. Expand
Structure of the Substrate Binding Domain of the Thermosome, an Archaeal Group II Chaperonin
TLDR
Models of the holochaperonin suggest a dual role of this helical protrusion in substrate binding and controlling access to the central cavity independent of a GroES-like cochaper onin. Expand
Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
TLDR
Improved refinement of the crystal structure of GroEL from Escherichia coli has resulted in a complete atomic model for the first 524 residues, indicating that conformational variability exists due to rigid-body movements between the apical and intermediate domains of Groel, resulting in deviations from strict seven-fold symmetry. Expand
Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCT
TLDR
The crystal structure of the thermosome, the archaeal group II chaperonin from T. acidophilum is determined to 2.6 A resolution and Binding of the transition state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds to the ATP form. Expand
The Crystal Structure of a GroEL/Peptide Complex Plasticity as a Basis for Substrate Diversity
TLDR
The structural analysis suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly. Expand
The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis
TLDR
The crystal structure of the proteolytic component of the caseinolytic Clp protease (ClpP) from E. coli is determined using an ab initio phasing procedure that exploits the internal 14-fold symmetry of the oligomer. Expand
3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin
TLDR
Three-dimensional reconstructions of apo- CCT and ATP-CCT have been obtained at 28 Å resolution by cryo-electron microscopy. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 46 REFERENCES
ATP induces large quaternary rearrangements in a cage-like chaperonin structure
TLDR
The observed rearrangement is consistent with an inward 5-10 degrees rotation of subunits, pivoting about the subunit contacts between the two heptamers, and thus bringing cpn60 domains towards the position occupied by the bound polypeptide. Expand
The symmetry of Escherichia coli cpn60 (GroEL) determined by X-ray crystallography.
TLDR
The internal symmetries of the Escherichia coli molecular chaperone cpn60 oligomer, also called GroEL, have been examined by X-ray crystallography and self-rotation functions calculated at a resolution of 8.9 A and shown to be valid also for the internal parts of GroEL and not only for surface views. Expand
Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.
TLDR
Chemical cross-linking and electron microscopy showed that in the presence of adenosine triphosphate (ATP), two GroES7 rings can successively bind a single GroEL14 core oligomer, which can nonetheless stably bind and assist the ATP-dependent refolding of RuBisCO enzyme. Expand
Symmetric complexes of GroE chaperonins as part of the functional cycle.
TLDR
The existence of symmetric chaperonin complexes is not predicted by current models of the functional cycle for GroE-mediated protein folding, but they are proposed to be functionally significant. Expand
Purification and properties of groE, a host protein involved in bacteriophage assembly.
  • R. Hendrix
  • Biology, Medicine
  • Journal of molecular biology
  • 1979
TLDR
A method is presented for the purification of gp groE, an Escherichia coli protein which is required for correct assembly of bacteriophages λ, T4, T5 and others, which is identical to a protein commonly found to copurify withRNA polymerase and which was originally misidentified as RNA polymerase. Expand
Residues in chaperonin GroEL required for polypeptide binding and release
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. Expand
The structure of interfaces between subunits of dimeric and tetrameric proteins.
  • S. Miller
  • Chemistry, Medicine
  • Protein engineering
  • 1989
TLDR
The structures of the interfaces of nine dimeric and nine tetrameric proteins have been analyzed and have been seen to follow general principles, including two-fold symmetry, charged hydrogen bonds and channel formation. Expand
A polypeptide bound by the chaperonin groEL is localized within a central cavity.
TLDR
It is concluded that folding intermediates are bound inside central cavities within individual chaperonin rings, in this potentially sequestered location, to facilitate rebinding of structures that initially fail to incorporate properly into the folding protein. Expand
Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
TLDR
Nuclear magnetic resonance techniques are used to show that the interaction of the small protein cyclophilin with GroEL is reversible by temperature changes, and all amide protons in GroEL-bound cyclophillin are exchanged with the solvent, although this exchange does not occur in free cyclophILin. Expand
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
TLDR
Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro and might represent a general mechanism for the formation of protein structure in vivo. Expand
...
1
2
3
4
5
...