Modulation of global low-frequency motions underlies allosteric regulation: demonstration in CRP/FNR family transcription factors.

ABSTRACT: Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distinct site. There is growing evidence that allosteric cooperativity can be communicated by modulation of protein dynamics without conformational change. The mechanisms, however, for communicating dynamic fluctuations between sites are debated. We provide a foundational theory for how allostery can occur as a function of low-frequency dynamics without a change in structure. We have generated coarse-grained models that describe the protein backbone motions of the CRP/FNR family transcription factors, CAP of Escherichia coli and GlxR of Corynebacterium glutamicum. The latter we demonstrate as a new exemplar for allostery without conformation change. We observe that binding the first molecule of

SUBMITTER: Rodgers TL 

PROVIDER: S-EPMC3769225 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature