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Nature. 1999 Dec 23-30;402(6764):894-8.

Structure of a transiently phosphorylated switch in bacterial signal transduction.

Author information

1
Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02454, USA. dkern@brandeis.edu

Abstract

Receiver 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.

PMID:
10622255
DOI:
10.1038/47273
[Indexed for MEDLINE]

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