1DC8

STRUCTURE OF A TRANSIENTLY PHOSPHORYLATED "SWITCH" IN BACTERIAL SIGNAL TRANSDUCTION

Summary for 1DC8

• Entry DOI: 10.2210/pdb1dc8/pdb
• Related: 1DC7 1NTR
• NMR Information: BMRB: 4528
• Descriptor: NITROGEN REGULATION PROTEIN (1 entity in total)
• Functional Keywords: receiver domain, phosphorylation, signal transduction, conformational rearrangement, two-component system, signaling protein
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 1
• Total formula weight: 13716.58

Authors

Kern, D.,Volkman, B.F.,Luginbuhl, P.,Nohaile, M.J.,Kustu, S.,Wemmer, D.E. (deposition date: 1999-11-04, release date: 2000-01-05, Last modification date: 2022-12-21)

Primary citation

Kern, D.,Volkman, B.F.,Luginbuhl, P.,Nohaile, M.J.,Kustu, S.,Wemmer, D.E.
Structure of a transiently phosphorylated switch in bacterial signal transduction.
Nature, 402:894-898, 1999

PubMed 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.

PubMed: 10622255
DOI: 10.1038/47273

Experimental method

SOLUTION NMR