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The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
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, asymmetricExpand
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The Hsp70 and Hsp60 Chaperone Machines
B. B. thanks members of his lab and J. Reinstein for critical reading of the manuscript and C. Gassler, T. Laufen, and S. Rudiger for figure preparation. A. H. thanks Wayne Fenton for criticalExpand
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Molecular Chaperones and Protein Quality Control
In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborateExpand
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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 subunitsExpand
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Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
The chaperonin GroEL is a double-ring structure with a central cavity in each ring that provides an environment for the efficient folding of proteins when capped by the co-chaperone GroES in theExpand
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ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy
The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneouslyExpand
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ClpS, a substrate modulator of the ClpAP machine.
In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. The mechanism by which these machines specifically recognizeExpand
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Loops in the Central Channel of ClpA Chaperone Mediate Protein Binding, Unfolding, and Translocation
The cylindrical Hsp100 chaperone ClpA mediates ATP-dependent unfolding of substrate proteins bearing "tag" sequences, such as the 11-residue ssrA sequence appended to proteins translationally stalledExpand
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Structure and function in GroEL-mediated protein folding.
Recent structural and biochemical investigations have come together to allow a better understanding of the mechanism of chaperonin (GroEL, Hsp60)-mediated protein folding, the final step in theExpand
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