Global low-frequency motions in protein allostery: CAP as a model system

Philip D. Townsend; Thomas L. Rodgers; Ehmke Pohl; Mark R. Wilson; Tom C B McLeish; Martin J. Cann

doi:10.1007/s12551-015-0163-9

Global low-frequency motions in protein allostery: CAP as a model system

Philip D. Townsend, Thomas L. Rodgers, Ehmke Pohl, Mark R. Wilson, Tom C B McLeish, Martin J. Cann^*

^*Corresponding author for this work

Physics

Research output: Contribution to journal › Article › peer-review

Abstract

Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of Escherichia coli is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding.

Original language	English
Pages (from-to)	175-182
Number of pages	8
Journal	Biophysical Reviews
Volume	7
Issue number	2
DOIs	https://doi.org/10.1007/s12551-015-0163-9
Publication status	Published - Jun 2015

Keywords

Allostery
Catabolite activator protein
Dynamics
Elastic network model
Normal modes
Protein

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10.1007/s12551-015-0163-9

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abstract = "Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of Escherichia coli is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding.",

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AU - Townsend, Philip D.

AU - Rodgers, Thomas L.

AU - Pohl, Ehmke

AU - Wilson, Mark R.

AU - McLeish, Tom C B

AU - Cann, Martin J.

PY - 2015/6

Y1 - 2015/6

N2 - Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of Escherichia coli is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding.

AB - Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of Escherichia coli is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding.

KW - Allostery

KW - Catabolite activator protein

KW - Dynamics

KW - Elastic network model

KW - Normal modes

KW - Protein

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JO - Biophysical Reviews

JF - Biophysical Reviews

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Global low-frequency motions in protein allostery: CAP as a model system

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Keywords

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