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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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Allosteric signaling of ATP hydrolysis in GroEL–GroES complexes
The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber,Expand
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The three-dimensional structure of genomic RNA in bacteriophage MS2: implications for assembly.
Using cryo-electron microscopy, single particle image processing and three-dimensional reconstruction with icosahedral averaging, we have determined the three-dimensional solution structure ofExpand
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Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy
PROTEIN folding mediated by the molecular chaperone GroEL occurs by its binding to non-native polypeptide substrates and is driven by ATP hydrolysis1. Both of these processes are influenced by theExpand
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The origins and consequences of asymmetry in the chaperonin reaction cycle.
The binding of nucleotides and chaperonin-10 (cpn10) to the Escherichia coli chaperonin-60 (cpn60) and their effect upon the molecular symmetry has been examined both kinetically and at equilibrium.Expand
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Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction.
Mitochondrial malate dehydrogenase (mMDH) folds more rapidly in the presence of GroEL, GroES and ATP than it does unassisted. The increase in folding rate as a function of the concentration ofExpand
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New Structural Insights into the Genome and Minor Capsid Proteins of BK Polyomavirus using Cryo-Electron Microscopy
Summary BK polyomavirus is the causative agent of several diseases in transplant patients and the immunosuppressed. In order to better understand the structure and life cycle of BK, we producedExpand
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An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology
Transmission electron microscopy (EM) is a versatile technique that can be used to image biological specimens ranging from intact eukaryotic cells to individual proteins >150 kDa. There are severalExpand
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Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM
The β-barrel assembly machinery (BAM) is a ∼203 kDa complex of five proteins (BamA–E), which is essential for viability in E. coli. BAM promotes the folding and insertion of β-barrel proteins intoExpand
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The Asymmetric Structure of an Icosahedral Virus Bound to Its Receptor Suggests a Mechanism for Genome Release
Summary Simple, spherical RNA viruses have well-understood, symmetric protein capsids, but little structural information is available for their asymmetric components, such as minor proteins and theirExpand
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