2ayy: Difference between revisions

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New page: left|200px<br /><applet load="2ayy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ayy" /> '''Solution structure of the E.coli RcsC C-term...
 
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[[Image:2ayy.gif|left|200px]]<br /><applet load="2ayy" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of the E.coli RcsC C-terminus (residues 700-816) containing linker region'''<br />


==Overview==
==Solution structure of the E.coli RcsC C-terminus (residues 700-816) containing linker region==
The Rcs signalling pathway controls a variety of physiological functions, like capsule synthesis, cell division or motility in prokaryotes. The Rcs, regulation cascade, involving a multi-step phosphorelay between the two, membrane-bound hybrid sensor kinases RcsC and RcsD and the global, regulator RcsB, is, up to now, one of the most complicated regulatory, systems in bacteria. To understand the structural basis of Rcs signal, transduction, NMR spectroscopy was employed to determine the solution, structure of the RcsC C terminus, possessing a phosphoreceiver domain, (RcsC-PR), and a region previously described as a long linker between the, histidine kinase domain of RcsC (RcsC-HK) and the RcsC-PR. We have found, that the linker region comprises an independent structural domain of a new, alpha/beta organization, which we named RcsC-ABL domain (Alpha/Beta/Loop)., The ABL domain appears to be a conserved and unique structural element of, RcsC-like kinases with no significant sequence homology to other proteins., The second domain of the C terminus, the RcsC-PR domain, represents a, well-folded CheY-like phosphoreceiver domain with the central parallel, beta-sheet covered with two alpha-helical layers on both sides. We have, mapped the interaction of RcsC-ABL and RcsC-PR with the histidine, phosphotransfer domain (HPt) of RcsD. In addition we have characterized, the interaction with and the conformational effects of Mg2+ and the, phosphorylation mimetic BeF(-)(3) on RcsC-ABL and RcsC-PR.
<StructureSection load='2ayy' size='340' side='right'caption='[[2ayy]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ayy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AYY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ayy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ayy OCA], [https://pdbe.org/2ayy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ayy RCSB], [https://www.ebi.ac.uk/pdbsum/2ayy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ayy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RCSC_ECOLI RCSC_ECOLI] Component of the Rcs signaling system, which controls transcription of numerous genes. RcsC functions as a membrane-associated protein kinase that phosphorylates RcsD in response to environmental signals. The phosphoryl group is then transferred to the response regulator RcsB. RcsC has also phosphatase activity. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.<ref>PMID:10564486</ref> <ref>PMID:11758943</ref> <ref>PMID:11309126</ref> <ref>PMID:11807084</ref> <ref>PMID:13129944</ref> <ref>PMID:14651646</ref>
== 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/ay/2ayy_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/main_output.php?pdb_ID=2ayy ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Rcs signalling pathway controls a variety of physiological functions like capsule synthesis, cell division or motility in prokaryotes. The Rcs regulation cascade, involving a multi-step phosphorelay between the two membrane-bound hybrid sensor kinases RcsC and RcsD and the global regulator RcsB, is, up to now, one of the most complicated regulatory systems in bacteria. To understand the structural basis of Rcs signal transduction, NMR spectroscopy was employed to determine the solution structure of the RcsC C terminus, possessing a phosphoreceiver domain (RcsC-PR), and a region previously described as a long linker between the histidine kinase domain of RcsC (RcsC-HK) and the RcsC-PR. We have found that the linker region comprises an independent structural domain of a new alpha/beta organization, which we named RcsC-ABL domain (Alpha/Beta/Loop). The ABL domain appears to be a conserved and unique structural element of RcsC-like kinases with no significant sequence homology to other proteins. The second domain of the C terminus, the RcsC-PR domain, represents a well-folded CheY-like phosphoreceiver domain with the central parallel beta-sheet covered with two alpha-helical layers on both sides. We have mapped the interaction of RcsC-ABL and RcsC-PR with the histidine phosphotransfer domain (HPt) of RcsD. In addition we have characterized the interaction with and the conformational effects of Mg2+ and the phosphorylation mimetic BeF(-)(3) on RcsC-ABL and RcsC-PR.


==About this Structure==
A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains.,Rogov VV, Rogova NY, Bernhard F, Koglin A, Lohr F, Dotsch V J Mol Biol. 2006 Nov 17;364(1):68-79. Epub 2006 Jul 29. PMID:17005198<ref>PMID:17005198</ref>
2AYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AYY OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains., Rogov VV, Rogova NY, Bernhard F, Koglin A, Lohr F, Dotsch V, J Mol Biol. 2006 Nov 17;364(1):68-79. Epub 2006 Jul 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17005198 17005198]
</div>
<div class="pdbe-citations 2ayy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bernhard, F.]]
[[Category: Bernhard F]]
[[Category: Dotsch, V.]]
[[Category: Dotsch V]]
[[Category: Koglin, A.]]
[[Category: Koglin A]]
[[Category: Lohr, F.]]
[[Category: Lohr F]]
[[Category: Rogov, V.V.]]
[[Category: Rogov VV]]
[[Category: Rogova, N.Y.]]
[[Category: Rogova NY]]
[[Category: alpha/beta layer]]
[[Category: new domain]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:28:19 2007''

Latest revision as of 14:19, 22 May 2024

Solution structure of the E.coli RcsC C-terminus (residues 700-816) containing linker regionSolution structure of the E.coli RcsC C-terminus (residues 700-816) containing linker region

Structural highlights

2ayy is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RCSC_ECOLI Component of the Rcs signaling system, which controls transcription of numerous genes. RcsC functions as a membrane-associated protein kinase that phosphorylates RcsD in response to environmental signals. The phosphoryl group is then transferred to the response regulator RcsB. RcsC has also phosphatase activity. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.[1] [2] [3] [4] [5] [6]

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 Rcs signalling pathway controls a variety of physiological functions like capsule synthesis, cell division or motility in prokaryotes. The Rcs regulation cascade, involving a multi-step phosphorelay between the two membrane-bound hybrid sensor kinases RcsC and RcsD and the global regulator RcsB, is, up to now, one of the most complicated regulatory systems in bacteria. To understand the structural basis of Rcs signal transduction, NMR spectroscopy was employed to determine the solution structure of the RcsC C terminus, possessing a phosphoreceiver domain (RcsC-PR), and a region previously described as a long linker between the histidine kinase domain of RcsC (RcsC-HK) and the RcsC-PR. We have found that the linker region comprises an independent structural domain of a new alpha/beta organization, which we named RcsC-ABL domain (Alpha/Beta/Loop). The ABL domain appears to be a conserved and unique structural element of RcsC-like kinases with no significant sequence homology to other proteins. The second domain of the C terminus, the RcsC-PR domain, represents a well-folded CheY-like phosphoreceiver domain with the central parallel beta-sheet covered with two alpha-helical layers on both sides. We have mapped the interaction of RcsC-ABL and RcsC-PR with the histidine phosphotransfer domain (HPt) of RcsD. In addition we have characterized the interaction with and the conformational effects of Mg2+ and the phosphorylation mimetic BeF(-)(3) on RcsC-ABL and RcsC-PR.

A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains.,Rogov VV, Rogova NY, Bernhard F, Koglin A, Lohr F, Dotsch V J Mol Biol. 2006 Nov 17;364(1):68-79. Epub 2006 Jul 29. PMID:17005198[7]

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

References

  1. ↑ Carballes F, Bertrand C, Bouche JP, Cam K. Regulation of Escherichia coli cell division genes ftsA and ftsZ by the two-component system rcsC-rcsB. Mol Microbiol. 1999 Nov;34(3):442-50. PMID:10564486
  2. ↑ Chen MH, Takeda S, Yamada H, Ishii Y, Yamashino T, Mizuno T. Characterization of the RcsC-->YojN-->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli. Biosci Biotechnol Biochem. 2001 Oct;65(10):2364-7. PMID:11758943
  3. ↑ Takeda S, Fujisawa Y, Matsubara M, Aiba H, Mizuno T. A novel feature of the multistep phosphorelay in Escherichia coli: a revised model of the RcsC --> YojN --> RcsB signalling pathway implicated in capsular synthesis and swarming behaviour. Mol Microbiol. 2001 Apr;40(2):440-50. PMID:11309126
  4. ↑ Clarke DJ, Joyce SA, Toutain CM, Jacq A, Holland IB. Genetic analysis of the RcsC sensor kinase from Escherichia coli K-12. J Bacteriol. 2002 Feb;184(4):1204-8. PMID:11807084
  5. ↑ Hagiwara D, Sugiura M, Oshima T, Mori H, Aiba H, Yamashino T, Mizuno T. Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB phosphorelay system in Escherichia coli. J Bacteriol. 2003 Oct;185(19):5735-46. PMID:13129944
  6. ↑ Ferrieres L, Clarke DJ. The RcsC sensor kinase is required for normal biofilm formation in Escherichia coli K-12 and controls the expression of a regulon in response to growth on a solid surface. Mol Microbiol. 2003 Dec;50(5):1665-82. PMID:14651646
  7. ↑ Rogov VV, Rogova NY, Bernhard F, Koglin A, Lohr F, Dotsch V. A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains. J Mol Biol. 2006 Nov 17;364(1):68-79. Epub 2006 Jul 29. PMID:17005198 doi:10.1016/j.jmb.2006.07.052
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