1dc7
STRUCTURE OF A TRANSIENTLY PHOSPHORYLATED "SWITCH" IN BACTERIAL SIGNAL TRANSDUCTIONSTRUCTURE OF A TRANSIENTLY PHOSPHORYLATED "SWITCH" IN BACTERIAL SIGNAL TRANSDUCTION
Structural highlights
FunctionNTRC_SALTY Member of the two-component regulatory system NtrB/NtrC involved in the activation of nitrogen assimilatory genes such as GlnA. NtrC is phosphorylated by NtrB and interacts with sigma-54. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedReceiver domains are the dominant molecular switches in bacterial signalling. Although several structures of non-phosphorylated receiver domains have been reported, a detailed structural understanding of the activation arising from phosphorylation has been impeded by the very short half-lives of the aspartylphosphate linkages. Here we present the first structure of a receiver domain in its active state, the phosphorylated receiver domain of the bacterial enhancer-binding protein NtrC (nitrogen regulatory protein C). Nuclear magnetic resonance spectra were taken during steady-state autophosphorylation/dephosphorylation, and three-dimensional spectra from multiple samples were combined. Phosphorylation induces a large conformational change involving a displacement of beta-strands 4 and 5 and alpha-helices 3 and 4 away from the active site, a register shift and an axial rotation in helix 4. This creates an exposed hydrophobic surface that is likely to transmit the signal to the transcriptional activation domain. Structure of a transiently phosphorylated switch in bacterial signal transduction.,Kern D, Volkman BF, Luginbuhl P, Nohaile MJ, Kustu S, Wemmer DE Nature. 1999 Dec 23-30;402(6764):894-8. PMID:10622255[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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