Structure of a transiently phosphorylated switch in bacterial signal transduction

Dorothee Kern (), Brian F. Volkman, Peter Luginbühl, Michael J. Nohaile, Sydney Kustu and David E. Wemmer
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Dorothee Kern: Brandeis University
Brian F. Volkman: National Magnetic Resonance Facility at Madison (NMRFAM), University of Wisconsin
Peter Luginbühl: Lawrence Berkeley National Laboratory and Department of Chemistry
Michael J. Nohaile: Lawrence Berkeley National Laboratory and Department of Chemistry
Sydney Kustu: University of California
David E. Wemmer: Lawrence Berkeley National Laboratory and Department of Chemistry

Nature, 1999, vol. 402, issue 6764, 894-898

Abstract: Abstract Receiver domains are the dominant molecular switches in bacterial signalling1,2. Although several structures of non-phosphorylated receiver domains have been reported3,4,5,6,7,8, a detailed structural understanding of the activation arising from phosphorylation has been impeded by the very short half-lives of the aspartyl-phosphate 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 β-strands 4 and 5 and α-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.

Date: 1999
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DOI: 10.1038/47273

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