2j6y: Difference between revisions
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New page: left|200px<br /><applet load="2j6y" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j6y, resolution 1.85Å" /> '''STRUCTURAL AND FUNCT... |
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== | ==Structural and Functional Characterisation of partner switching regulating the environmental stress response in Bacillus subtilis== | ||
<StructureSection load='2j6y' size='340' side='right'caption='[[2j6y]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2j6y]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J6Y FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</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=2j6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j6y OCA], [https://pdbe.org/2j6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j6y RCSB], [https://www.ebi.ac.uk/pdbsum/2j6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j6y ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RSBU_BACSU RSBU_BACSU] Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module.<ref>PMID:8824586</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/j6/2j6y_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=2j6y ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The general stress response of Bacillus subtilis and close relatives provides the cell with protection from a variety of stresses. The upstream component of the environmental stress signal transduction cascade is activated by the RsbT kinase that switches binding partners from a 25 S macromolecular complex, the stressosome, to the RsbU phosphatase. Once the RsbU phosphatase is activated by interacting with RsbT, the alternative sigma factor, sigmaB, directs transcription of the general stress regulon. Previously, we demonstrated that the N-terminal domain of RsbU mediates the binding of RsbT. We now describe residues in N-RsbU that are crucial to this interaction by experimentation both in vitro and in vivo. Furthermore, crystal structures of the N-RsbU mutants provide a molecular explanation for the loss of interaction. Finally, we also characterize mutants in RsbT that affect binding to both RsbU and a simplified, binary model of the stressosome and thus identify overlapping binding surfaces on the RsbT "switch." | |||
Structural and functional characterization of partner switching regulating the environmental stress response in Bacillus subtilis.,Hardwick SW, Pane-Farre J, Delumeau O, Marles-Wright J, Murray JW, Hecker M, Lewis RJ J Biol Chem. 2007 Apr 13;282(15):11562-72. Epub 2007 Feb 15. PMID:17303566<ref>PMID:17303566</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2j6y" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphoserine phosphatase|Phosphoserine phosphatase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Delumeau O]] | |||
[[Category: Delumeau | [[Category: Hardwick SW]] | ||
[[Category: Hardwick | [[Category: Hecker M]] | ||
[[Category: Hecker | [[Category: Lewis RJ]] | ||
[[Category: Lewis | [[Category: Marles-Wright J]] | ||
[[Category: Marles-Wright | [[Category: Murray JW]] | ||
[[Category: Murray | [[Category: Pane-Farre J]] | ||
[[Category: Pane-Farre | |||
Latest revision as of 17:36, 13 December 2023
Structural and Functional Characterisation of partner switching regulating the environmental stress response in Bacillus subtilisStructural and Functional Characterisation of partner switching regulating the environmental stress response in Bacillus subtilis
Structural highlights
FunctionRSBU_BACSU Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module.[1] 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 PubMedThe general stress response of Bacillus subtilis and close relatives provides the cell with protection from a variety of stresses. The upstream component of the environmental stress signal transduction cascade is activated by the RsbT kinase that switches binding partners from a 25 S macromolecular complex, the stressosome, to the RsbU phosphatase. Once the RsbU phosphatase is activated by interacting with RsbT, the alternative sigma factor, sigmaB, directs transcription of the general stress regulon. Previously, we demonstrated that the N-terminal domain of RsbU mediates the binding of RsbT. We now describe residues in N-RsbU that are crucial to this interaction by experimentation both in vitro and in vivo. Furthermore, crystal structures of the N-RsbU mutants provide a molecular explanation for the loss of interaction. Finally, we also characterize mutants in RsbT that affect binding to both RsbU and a simplified, binary model of the stressosome and thus identify overlapping binding surfaces on the RsbT "switch." Structural and functional characterization of partner switching regulating the environmental stress response in Bacillus subtilis.,Hardwick SW, Pane-Farre J, Delumeau O, Marles-Wright J, Murray JW, Hecker M, Lewis RJ J Biol Chem. 2007 Apr 13;282(15):11562-72. Epub 2007 Feb 15. PMID:17303566[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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