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| | <StructureSection load='2j70' size='340' side='right'caption='[[2j70]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='2j70' size='340' side='right'caption='[[2j70]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2j70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J70 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2j70]] is a 1 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=2J70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J70 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1w53|1w53]], [[2j6y|2j6y]], [[2j6z|2j6z]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span></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=2j70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j70 OCA], [https://pdbe.org/2j70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j70 RCSB], [https://www.ebi.ac.uk/pdbsum/2j70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j70 ProSAT]</span></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=2j70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j70 OCA], [https://pdbe.org/2j70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j70 RCSB], [https://www.ebi.ac.uk/pdbsum/2j70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j70 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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>
| + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoserine phosphatase]]
| + | [[Category: Delumeau O]] |
| - | [[Category: Delumeau, O]] | + | [[Category: Hardwick SW]] |
| - | [[Category: Hardwick, S W]] | + | [[Category: Hecker M]] |
| - | [[Category: Hecker, M]] | + | [[Category: Lewis RJ]] |
| - | [[Category: Lewis, R J]] | + | [[Category: Marles-Wright J]] |
| - | [[Category: Marles-Wright, J]] | + | [[Category: Murray JW]] |
| - | [[Category: Murray, J W]] | + | [[Category: Pane-Farre J]] |
| - | [[Category: Pane-Farre, J]] | + | |
| - | [[Category: Bacillus subtili]]
| + | |
| - | [[Category: Environmental stress response]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Partner switching]]
| + | |
| - | [[Category: Protein phosphatase]]
| + | |
| - | [[Category: Rsbt]]
| + | |
| - | [[Category: Rsbu]]
| + | |
| Structural highlights
Function
RSBU_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 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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yang X, Kang CM, Brody MS, Price CW. Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor. Genes Dev. 1996 Sep 15;10(18):2265-75. PMID:8824586
- ↑ Hardwick SW, Pane-Farre J, Delumeau O, Marles-Wright J, Murray JW, Hecker M, Lewis RJ. Structural and functional characterization of partner switching regulating the environmental stress response in Bacillus subtilis. J Biol Chem. 2007 Apr 13;282(15):11562-72. Epub 2007 Feb 15. PMID:17303566 doi:10.1074/jbc.M609733200
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