2w0n

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{{STRUCTURE_2w0n| PDB=2w0n | SCENE= }}
 
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===Plasticity of PAS domain and potential role for signal transduction in the histidine-kinase DcuS===
 
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{{ABSTRACT_PUBMED_18820688}}
 
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==Function==
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==Plasticity of PAS domain and potential role for signal transduction in the histidine-kinase DcuS==
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[[http://www.uniprot.org/uniprot/DCUS_ECOLI DCUS_ECOLI]] Member of the two-component regulatory system DcuR/DcuS. Involved in the C4-dicarboxylate-stimulated regulation of the genes encoding the anaerobic fumarate respiratory system (frdABCD; nuoAN; dcuB; dcuC; sdhCDAB; etc.). Weakly regulates the aerobic C4-dicarboxylate transporter dctA. Activates DcuR by phosphorylation.
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<StructureSection load='2w0n' size='340' side='right'caption='[[2w0n]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2w0n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W0N FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ojg|1ojg]]</div></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0n OCA], [https://pdbe.org/2w0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w0n RCSB], [https://www.ebi.ac.uk/pdbsum/2w0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w0n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/DCUS_ECOLI DCUS_ECOLI]] Member of the two-component regulatory system DcuR/DcuS. Involved in the C4-dicarboxylate-stimulated regulation of the genes encoding the anaerobic fumarate respiratory system (frdABCD; nuoAN; dcuB; dcuC; sdhCDAB; etc.). Weakly regulates the aerobic C4-dicarboxylate transporter dctA. Activates DcuR by phosphorylation.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w0/2w0n_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2w0n ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mechanistic understanding of how membrane-embedded sensor kinases recognize signals and regulate kinase activity is currently limited. Here we report structure-function relationships of the multidomain membrane sensor kinase DcuS using solid-state NMR, structural modeling and mutagenesis. Experimental data of an individual cytoplasmic Per-Arnt-Sim (PAS) domain were compared to structural models generated in silico. These studies, together with previous NMR work on the periplasmic PAS domain, enabled structural investigations of a membrane-embedded 40-kDa construct by solid-state NMR, comprising both PAS segments and the membrane domain. Structural alterations are largely limited to protein regions close to the transmembrane segment. Data from isolated and multidomain constructs favor a disordered N-terminal helix in the cytoplasmic domain. Mutations of residues in this region strongly influence function, suggesting that protein flexibility is related to signal transduction toward the kinase domain and regulation of kinase activity.
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==About this Structure==
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Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS.,Etzkorn M, Kneuper H, Dunnwald P, Vijayan V, Kramer J, Griesinger C, Becker S, Unden G, Baldus M Nat Struct Mol Biol. 2008 Oct;15(10):1031-9. Epub 2008 Sep 28. PMID:18820688<ref>PMID:18820688</ref>
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[[2w0n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W0N OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:018820688</ref><references group="xtra"/><references/>
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</div>
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<div class="pdbe-citations 2w0n" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus coli migula 1895]]
[[Category: Histidine kinase]]
[[Category: Histidine kinase]]
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[[Category: Baldus, M.]]
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[[Category: Large Structures]]
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[[Category: Becker, S.]]
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[[Category: Baldus, M]]
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[[Category: Duennwald, P.]]
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[[Category: Becker, S]]
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[[Category: Etzkorn, M.]]
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[[Category: Duennwald, P]]
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[[Category: Griesinger, C.]]
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[[Category: Etzkorn, M]]
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[[Category: Kneuper, H.]]
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[[Category: Griesinger, C]]
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[[Category: Kraemer, J.]]
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[[Category: Kneuper, H]]
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[[Category: Unden, G.]]
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[[Category: Kraemer, J]]
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[[Category: Vijayan, V.]]
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[[Category: Unden, G]]
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[[Category: Vijayan, V]]
[[Category: Cell inner membrane]]
[[Category: Cell inner membrane]]
[[Category: Cell membrane]]
[[Category: Cell membrane]]

Current revision

Plasticity of PAS domain and potential role for signal transduction in the histidine-kinase DcuS

PDB ID 2w0n

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