1dc8: Difference between revisions
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[[Image: | ==STRUCTURE OF A TRANSIENTLY PHOSPHORYLATED "SWITCH" IN BACTERIAL SIGNAL TRANSDUCTION== | ||
<StructureSection load='1dc8' size='340' side='right' caption='[[1dc8]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1dc8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DC8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DC8 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ntr|1ntr]], [[1dc7|1dc7]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dc8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dc8 RCSB], [http://www.ebi.ac.uk/pdbsum/1dc8 PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dc/1dc8_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:10622255</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | [[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | ||
[[Category: Kern, D.]] | [[Category: Kern, D.]] | ||
Revision as of 06:42, 4 September 2014
STRUCTURE OF A TRANSIENTLY PHOSPHORYLATED "SWITCH" IN BACTERIAL SIGNAL TRANSDUCTION
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