期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 63, 期 4, 页码 846-867出版社
WILEY
DOI: 10.1002/prot.20893
关键词
signal transduction; structural flexibility; allosteric transition; induced fit; population shift; molecular dynamics
资金
- NIGMS NIH HHS [R01-GM071428] Funding Source: Medline
A combination of thirty-two 10-ns-scale molecular dynamics simulations were used to explore the coupling between conformational. transition and phosphorylation in the bacteria chemotaxis Y protein (CheY), as a simple but representative example of protein allostery. Results from these simulations support an activation mechanism in which the beta 4-alpha 4 loop, at least partially, gates the isomerization. of Tyr106. The roles of phosphorylation and the conserved Thr87 are deemed indirect in that they stabilize the active configuration of the beta 4-alpha 4 loop. The indirect role of the activation event (phosphorylation) and/or conserved residues in stabilizing, rather than causing, specific conformational transition is likely a feature in many signaling systems. The current analysis of CheY also helps to make clear that neither the old (induced fit) nor the new (population shift) views for protein allostery are complete, because they emphasize the kinetic (mechanistic) and thermodynamic aspects of allosteric transitions, respectively. In this regard, an issue that warrants further analysis concerns the interplay of concerted collective motion and sequential local structural changes in modulating cooperativity between distant sites in biomolecules.
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