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Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes?

McLeish, T.C.B.; Cann, M.J.; Rodgers, T.L.

Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes? Thumbnail


Authors

T.C.B. McLeish

T.L. Rodgers



Abstract

We examine the contrast between mechanisms for allosteric signaling that involve structural change, and those that do not, from the perspective of allosteric pathways. In particular we treat in detail the case of fluctuation-allostery by which amplitude modulation of the thermal fluctuations of the elastic normal modes conveys the allosteric signal, and address the question of what an allosteric pathway means in this case. We find that a perturbation theory of thermal elastic solids and nonperturbative approach (by super-coarse-graining elasticity into internal bending modes) have opposite signatures in their structure of correlated pathways. We illustrate the effect from analysis of previous results from GlxR of Corynebacterium glutamicum, an example of the CRP/FNR transcription family of allosteric homodimers. We find that the visibility of both correlated pathways and disconnected sites of correlated motion in this protein suggests that mechanisms of local elastic stretch and bend are recruited for the purpose of creating and controlling allosteric cooperativity.

Citation

McLeish, T., Cann, M., & Rodgers, T. (2015). Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes?. Biophysical Journal, 109(6), 1240-1250. https://doi.org/10.1016/j.bpj.2015.08.009

Journal Article Type Article
Acceptance Date Aug 7, 2015
Online Publication Date Aug 31, 2015
Publication Date Sep 15, 2015
Deposit Date Sep 18, 2015
Publicly Available Date Mar 28, 2024
Journal Biophysical Journal
Print ISSN 0006-3495
Publisher Biophysical Society
Peer Reviewed Peer Reviewed
Volume 109
Issue 6
Pages 1240-1250
DOI https://doi.org/10.1016/j.bpj.2015.08.009

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