1dc8
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(New page: 200px<br /><applet load="1dc8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dc8" /> '''STRUCTURE OF A TRANSIENTLY PHOSPHORYLATED "S...)
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Revision as of 11:02, 20 November 2007
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STRUCTURE OF A TRANSIENTLY PHOSPHORYLATED "SWITCH" IN BACTERIAL SIGNAL TRANSDUCTION
Overview
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.
About this Structure
1DC8 is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
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
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