Energetics of nucleotide-induced DnaK conformational states.

Stefka Germanova Taneva, Fernando Moro, Adrian Velazquez-Campoy, Arturo Muga
Published 2010 in Biochemistry

Abstract

Hsp70 chaperones are molecular switches that use the free energy of ATP binding and hydrolysis to modulate their affinity for protein substrates and, most likely, to remodel non-native interactions allowing proper substrate folding. By means of isothermal titration calorimetry, we have measured the thermodynamics of ATP and ADP binding to (i) wild-type DnaK… (More)

DOI: 10.1021/bi901847q

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The allosteric transition in DnaK probed by infrared difference spectroscopy. Concerted ATP-induced rearrangement of the substrate binding domain.

Fernando Moro, Vanesa Fernández-Sáiz, Arturo Muga
Protein science : a publication of the Protein…
2006

Energetics of nucleotide-induced DnaK conformational states.

Abstract

Topics

6 Figures and Tables

Statistics

Citation Velocity: 15

Cited By

Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulation

Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions

Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and Communication

The intervening domain from MeCP2 enhances the DNA affinity of the methyl binding domain and provides an independent DNA interaction site

A Spatial Control for Correct Timing of Gene Expression during the Escherichia coli Cell Cycle

Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE.

Substrate-binding domain conformational dynamics mediate Hsp70 allostery.

Specialized Hsp70 Chaperone (HscA) Binds Preferentially to the Disordered Form, whereas J-protein (HscB) Binds Preferentially to the Structured Form of the Iron-Sulfur Cluster Scaffold Protein (IscU)*

Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones.

Conformational Sampling and Nucleotide-Dependent Transitions of the GroEL Subunit Probed by Unbiased Molecular Dynamics Simulations

References

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.

Thermodynamics of zinc binding to hepatitis C virus NS3 protease: a folding by binding event.

Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker.

Allosteric regulation of Hsp70 chaperones by a proline switch.

Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker.

Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation.

Molecular Chaperones and Protein Quality Control

The allosteric transition in DnaK probed by infrared difference spectroscopy. Concerted ATP-induced rearrangement of the substrate binding domain.

The native-state ensemble of proteins provides clues for folding, misfolding and function.

Switches, catapults, and chaperones: steady-state kinetic analysis of Hsp70-substrate interactions.

Slides referencing similar topics

Energetics of nucleotide-induced DnaK conformational states.

Abstract

Topics

6 Figures and Tables

Statistics

Citation Velocity: 15

Cited By

Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulation

Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions

Computational Analysis of Residue Interaction Networks and Coevolutionary Relationships in the Hsp70 Chaperones: A Community-Hopping Model of Allosteric Regulation and Communication

The intervening domain from MeCP2 enhances the DNA affinity of the methyl binding domain and provides an independent DNA interaction site

A Spatial Control for Correct Timing of Gene Expression during the Escherichia coli Cell Cycle

Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE.

Substrate-binding domain conformational dynamics mediate Hsp70 allostery.

Specialized Hsp70 Chaperone (HscA) Binds Preferentially to the Disordered Form, whereas J-protein (HscB) Binds Preferentially to the Structured Form of the Iron-Sulfur Cluster Scaffold Protein (IscU)*

Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones.

Conformational Sampling and Nucleotide-Dependent Transitions of the GroEL Subunit Probed by Unbiased Molecular Dynamics Simulations

References

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.

Thermodynamics of zinc binding to hepatitis C virus NS3 protease: a folding by binding event.

Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker.

Allosteric regulation of Hsp70 chaperones by a proline switch.

Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker.

Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation.

Molecular Chaperones and Protein Quality Control

The allosteric transition in DnaK probed by infrared difference spectroscopy. Concerted ATP-induced rearrangement of the substrate binding domain.

The native-state ensemble of proteins provides clues for folding, misfolding and function.

Switches, catapults, and chaperones: steady-state kinetic analysis of Hsp70-substrate interactions.

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Slides referencing similar topics