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.
Highlights
Allostery (from the Greek allos stereos Bother solid^) is the regulation of protein function through the binding of an effector molecule at a site other than the protein’s functional site (Cornish-Bowden 2014)
Allostery is the regulation of protein function through the binding of an effector molecule at a site other than the protein’s functional site (Cornish-Bowden 2014)
A significant issue arises with understanding the theoretical underpinning of allostery in Catabolite Activator Protein (CAP) as a number of hypotheses have been presented to explain the mechanism by which dynamic fluctuations are communicated between allosterically coupled sites in various protein systems
Summary
Allostery (from the Greek allos stereos Bother solid^) is the regulation of protein function through the binding of an effector molecule at a site other than the protein’s functional site (Cornish-Bowden 2014). Subsequent theoretical developments have emphasised the role of ligand-modulated low-frequency global modes of protein dynamics in generating allosteric interaction between distant binding sites (Hawkins and McLeish 2004, 2006a). The suppression of the μs–ms range motions on binding the second molecule of cAMP represents the entropic penalty that is the source of negative co-operativity and the study overall demonstrated that allostery can arise through a purely dynamic mechanism.
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