Molecular strategies for phosphorylation-mediated regulation of response regulator activity.
Response regulator (RR) proteins exploit different molecular surfaces in their inactive and active conformations for a variety of regulatory intramolecular and/or intermolecular protein-protein interactions that either inhibit or activate effector domain activities. This versatile strategy enables numerous regulatory mechanisms among RRs. The recent accumulation of structures of inactive and active forms of multidomain RRs and RR complexes has revealed many different domain arrangements that have provided insight into regulatory mechanisms. Although diversity is the rule, even among subfamily members containing homologous domains, several structural modes of interaction and mechanisms of regulation recur frequently. These themes involve interactions at the alpha4-beta5-alpha5 face of the receiver domain, modes of dimerization of receiver domains, and inhibitory or activating heterodomain interactions.
Gao
Rong
R
Center for Advanced Biotechnology and Medicine, UMDNJ-Robert Wood Johnson, Medical School and Howard Hughes Medical Institute, Piscataway, NJ, USA.
Stock
Ann M
AM
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D001665:Binding Sites; D020134:Catalytic Domain; D019281:Dimerization; D015964:Gene Expression Regulation, Bacterial; D008958:Models, Molecular; D010766:Phosphorylation; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D014157:Transcription Factors