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2w0n

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Revision as of 21:22, 19 September 2018

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

Structural highlights

2w0n is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1ojg
Activity:	Histidine kinase, with EC number 2.7.13.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Etzkorn M, Kneuper H, Dunnwald P, Vijayan V, Kramer J, Griesinger C, Becker S, Unden G, Baldus M. Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS. Nat Struct Mol Biol. 2008 Oct;15(10):1031-9. Epub 2008 Sep 28. PMID:18820688 doi:10.1038/nsmb.1493

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2w0n"

@@ Line 1: / Line 1: @@
 ==Plasticity of PAS domain and potential role for signal transduction in the histidine-kinase DcuS==
 <StructureSection load='2w0n' size='340' side='right' caption='[[2w0n]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ojg|1ojg]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0n OCA], [http://pdbe.org/2w0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w0n RCSB], [http://www.ebi.ac.uk/pdbsum/2w0n PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w0n OCA], [http://pdbe.org/2w0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w0n RCSB], [http://www.ebi.ac.uk/pdbsum/2w0n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2w0n ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w0/2w0n_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w0/2w0n_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2w0n

From Proteopedia

Revision as of 21:22, 19 September 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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