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Identification of communication networks in Spo0F: a model for phosphorylation-induced conformational change and
V A Feher1, Y L Tzeng, J A Hoch
1NMR Structural Biology Facility, Wadsworth Center, New York State Department of Health, Albany 12201, USA.
Abstract:
Fundamental to understanding the mechanism by which phosphorylation activates bacterial signal transduction response regulator proteins is the identification of regions and residues that are responsible for the phosphorylation-induced conformational change. Here we review results from structural and protein dynamics investigations, and combine them with mutagenesis studies on the response regulator protein SpoOF to suggest a model in which a network of buried and surface residues link surface regions required for protein:protein interactions to the site of phosphorylation. The network described for SpoOF may provide pathways through which information is transmitted from the site of phosphorylation, propagating a conformational change many angstroms away. The general applicability of the communication network model for all bacterial response regulator proteins is discussed.