Crystal structure of wild-type chaperonin GroEL.

No abstract is available for this paper.

• Publication year

  2005

• Venue

  Journal of Molecular Biology

• Publication date

  2005-12-09

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/J.JMB.2005.09.096PMID 16288915
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis

  2005cited by this paper
• The 13 Å Structure of a Chaperonin GroEL–Protein Substrate Complex by Cryo-electron Microscopy

  2005cited by this paper
• The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy.

  2005cited by this paper
• A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation

  2004cited by this paper
• Kinetic analysis of ATP-dependent inter-ring communication in GroEL.

  2004cited by this paper
• Domain motions in GroEL upon binding of an oligopeptide.

  2003cited by this paper
• STRUCTURAL BASIS FOR GROEL-ASSISTED PROTEIN FOLDING FROM THE CRYSTAL STRUCTURE OF (GROEL-KMGATP) 14 AT 2.0 ANGSTROM RESOLUTION

  2003cited by this paper
• Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution.

  2003cited by this paper
• Conversion of the allosteric transition of GroEL from concerted to sequential by the single mutation Asp-155 → Ala

  2003cited by this paper
• Role of the γ‐phosphate of ATP in triggering protein folding by GroEL–GroES: function, structure and energetics

  2003influential reference
• Salt Bridges at the Inter-ring Interface Regulate the Thermostat of GroEL*

  2002cited by this paper
• Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations

  2002cited by this paper
• Synchronized Domain-opening Motion of GroEL Is Essential for Communication between the Two Rings*

  2001cited by this paper
• Review: a structural view of the GroE chaperone cycle.

  2001cited by this paper
• ATP-bound states of GroEL captured by cryo-electron microscopy.

  2001influential reference
• Review: allostery in chaperonins.

  2001cited by this paper
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  2000cited by this paper
• A Dynamic Model for the Allosteric Mechanism of GroEL

  2000cited by this paper
• A dynamic model for the allosteric mechanism of GroEL.

  2000cited by this paper
• The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

  1999cited by this paper
• An arginine residue (Arg101), which is conserved in many GroEL homologues, is required for interactions between the two heptameric rings.

  1998cited by this paper
• Crystallography & NMR system: A new software suite for macromolecular structure determination.

  1998cited by this paper
• The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

  1997influential reference
• Processing of X-ray diffraction data collected in oscillation mode.

  1997influential reference
• The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

  1996cited by this paper
• Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure.

  1996influential reference
• Allosteric control by ATP of non-folded protein binding to GroEL.

  1996cited by this paper
• Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution

  1995cited by this paper
• Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

  1994cited by this paper
• Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex.

  1994cited by this paper
• Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement

  1994cited by this paper
• AMoRe: an automated package for molecular replacement

  1994cited by this paper
• The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

  1994cited by this paper
• Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement

  1991influential reference
• Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition.

  1990cited by this paper
• Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.

  1990cited by this paper
• Strength and co-operativity of contributions of surface salt bridges to protein stability.

  1990cited by this paper
• The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

  1989cited by this paper
• Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes

  1986cited by this paper

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  2025cites this paper
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• From Microstates to Macrostates in the Conformational Dynamics of GroEL: a Single-Molecule FRET Study

  2023cites this paper
• Evaluation and Characterization of the Insecticidal Activity and Synergistic Effects of Different GroEL Proteins from Bacteria Associated with Entomopathogenic Nematodes on Galleria mellonella

  2023cites this paper
• Three-dimensional motions of GroEL during substrate protein recognition

  2022cites this paper
• Single-molecule 3D imaging of HIV cellular entry by liquid-phase electron tomography

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• Local Flexibility of a New Single-Ring Chaperonin Encoded by Bacteriophage AR9 Bacillus subtilis

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• Cryo-EM Analyses Permit Visualization of Structural Polymorphism of Biological Macromolecules

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  2021cites this paper
• Temperature Regulates Stability, Ligand Binding (Mg2+ and ATP), and Stoichiometry of GroEL-GroES Complexes.

  2021cites this paper
• Probing the Interaction of Huntingtin Exon‐1 Polypeptides with the Chaperonin Nanomachine GroEL

  2021cites this paper
• Exome sequencing revealed a novel homozygous METTL23 gene mutation leading to familial mild intellectual disability with dysmorphic features.

  2020cites this paper
• Structure and conformational cycle of a bacteriophage-encoded chaperonin

  2020cites this paper
• Cryo-EM structure of human mitochondrial HSPD1

  2020cites this paper
• Crystal Structure of Chaperonin GroEL from Xanthomonas oryzae pv. oryzae

  2019cites this paper
• Protein Supersecondary Structures

  2019cites this paper
• Homology Searches Using Supersecondary Structure Code.

  2019cites this paper
• Cryo-EM reveals an asymmetry in a novel single-ring viral chaperonin.

  2019cites this paper
• The GroEL chaperonin: a protein machine with pistons driven by ATP binding and hydrolysis

  2018cites this paper
• Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.

  2018cites this paper
• The determinant factors for map resolutions obtained using CryoEM single particle imaging method

  2018cites this paper
• Structure Resource Tracing Beta Strands Using StrandTwister from Cryo-EM Density Maps at Medium Resolutions

  2018cites this paper
• Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM

  2017influential citation
• Simultaneous Determination of Protein Structure and Dynamics Using Cryo-Electron Microscopy

  2017influential citation
• The determinant factors for model resolutions obtained using CryoEM method

  2017cites this paper
• Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein

  2017cites this paper
• Long Distance Measurements up to 160 Å in the GroEL Tetradecamer Using Q-Band DEER EPR Spectroscopy.

  2016cites this paper
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  2016cites this paper
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  2016cites this paper
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  2016cites this paper
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  2016cites this paper
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  2016cites this paper
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  2016cites this paper
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  2012cites this paper
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  2012cites this paper
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  2012cites this paper
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  2011cites this paper
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  2008cites this paper
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  2008cites this paper
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  2007influential citation
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  2007cites this paper
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  2006cites this paper
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