Synchrotron protein footprinting supports substrate translocation by ClpA via ATP-induced movements of the D2 loop.

No abstract is available for this paper.

• Publication year

  2008

• Venue

  Structure

• Publication date

  2008-08-06

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.str.2008.04.016PMID 18682217PMCID PMC2929679
• 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.

• Installation and testing of a focusing mirror at beamline X28C for high flux x-ray radiolysis of biological macromolecules.

  2008influential reference
• Complementary structural mass spectrometry techniques reveal local dynamics in functionally important regions of a metastable serpin.

  2008cited by this paper
• Single-molecule analysis of nucleotide-dependent substrate binding by the protein unfoldase ClpA.

  2007cited by this paper
• The Beamline X28C of the Center for Synchrotron Biosciences: a national resource for biomolecular structure and dynamics experiments using synchrotron footprinting.

  2007cited by this paper
• Hydroxyl radical-mediated modification of proteins as probes for structural proteomics.

  2007cited by this paper
• Modeling AAA+ ring complexes from monomeric structures.

  2006cited by this paper
• The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes.

  2006cited by this paper
• Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site.

  2006cited by this paper
• Radiolytic modification and reactivity of amino acid residues serving as structural probes for protein footprinting.

  2005cited by this paper
• The Molecular Chaperone, ClpA, Has a Single High Affinity Peptide Binding Site per Hexamer*

  2005cited by this paper
• Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation.

  2005influential reference
• Secondary reactions and strategies to improve quantitative protein footprinting.

  2005cited by this paper
• Control of peptide product sizes by the energy-dependent protease ClpAP.

  2005cited by this paper
• Dysregulation of bacterial proteolytic machinery by a new class of antibiotics

  2005cited by this paper
• Coot: model-building tools for molecular graphics.

  2004cited by this paper
• Monovalent ion-mediated folding of the Tetrahymena thermophila ribozyme.

  2004cited by this paper
• Communication between ClpX and ClpP during substrate processing and degradation

  2004cited by this paper
• The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP protease.

  2004cited by this paper
• Crystal Structure of ClpA, an Hsp100 Chaperone and Regulator of ClpAP Protease*

  2002influential reference
• Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry

  2002cited by this paper
• Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase

  2001cited by this paper
• Functional Domains of the ClpA and ClpX Molecular Chaperones Identified by Limited Proteolysis and Deletion Analysis*

  2001cited by this paper
• Conditional Stability of the HemA Protein (Glutamyl-tRNA Reductase) Regulates Heme Biosynthesis inSalmonella typhimurium

  1999cited by this paper
• Global unfolding of a substrate protein by the Hsp100 chaperone ClpA

  1999cited by this paper
• ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease.

  1999cited by this paper
• The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system.

  1998cited by this paper
• RNA folding at millisecond intervals by synchrotron hydroxyl radical footprinting.

  1998cited by this paper
• Enzymatic and Structural Similarities between theEscherichia coli ATP-dependent Proteases, ClpXP and ClpAP*

  1998cited by this paper
• Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP.

  1998cited by this paper
• At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease.

  1998cited by this paper
• The role of the ClpA chaperone in proteolysis by ClpAP.

  1998cited by this paper
• The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis.

  1997cited by this paper
• Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome.

  1995cited by this paper
• A molecular chaperone, ClpA, functions like DnaK and DnaJ.

  1994cited by this paper
• The 65-kDa protein derived from the internal translational initiation site of the clpA gene inhibits the ATP-dependent protease Ti in Escherichia coli.

  1994cited by this paper
• The CCP4 suite: programs for protein crystallography.

  1994cited by this paper
• Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli.

  1994cited by this paper
• Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis.

  1994cited by this paper
• Role of Clp protease subunits in degradation of carbon starvation proteins in Escherichia coli

  1993cited by this paper
• ATP-promoted interaction between Clp A and Clp P in activation of Clp protease from Escherichia coli.

  1991cited by this paper
• The N-end rule in bacteria.

  1991cited by this paper
• Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La.

  1987cited by this paper

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  2025cites this paper
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  2023cites this paper
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  2019cites this paper
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  2019cites this paper
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  2019cites this paper
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  2019cites this paper
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  2019cites this paper
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  2017cites this paper
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  2017cites this paper
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  2016cites this paper
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  2016cites this paper
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  2016cites this paper
• Protein Structure and Folding

  2016cites this paper
• Structural Features Reminiscent of ATP-Driven Protein Translocases Are Essential for the Function of a Type III Secretion-Associated ATPase

  2015cites this paper
• Oxidative footprinting in the study of structure and function of membrane proteins: current state and perspectives.

  2015cites this paper
• Oxidative Protein Labeling with Analysis by Mass Spectrometry for the Study of Structure, Folding, and Dynamics

  2014cites this paper
• ATPγS competes with ATP for binding at Domain 1 but not Domain 2 during ClpA catalyzed polypeptide translocation.

  2014cites this paper
• Synchrotron X-ray footprinting on tour.

  2014influential citation
• Structural and functional studies of the ATP-dependent Clp proteases in cyanobacteria

  2014cites this paper
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  2014influential citation
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  2014cites this paper
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  2013cites this paper
• Examination of the polypeptide substrate specificity for Escherichia coli ClpA.

  2013cites this paper
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  2013cites this paper
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  2013cites this paper
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  2013cites this paper
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  2011cites this paper
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  2010cites this paper
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  2009cites this paper
• Mapping protein-protein interactions by localized oxidation: consequences of the reach of hydroxyl radical.

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  2008cites this paper