1w53

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[[Image:1w53.gif|left|200px]]
 
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==Kinase recruitment domain of the stress phosphatase RsbU==
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The line below this paragraph, containing "STRUCTURE_1w53", creates the "Structure Box" on the page.
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<StructureSection load='1w53' size='340' side='right'caption='[[1w53]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1w53]] 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=1W53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W53 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
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{{STRUCTURE_1w53| PDB=1w53 | SCENE= }}
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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=1w53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w53 OCA], [https://pdbe.org/1w53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w53 RCSB], [https://www.ebi.ac.uk/pdbsum/1w53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w53 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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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/w5/1w53_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=1w53 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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RsbU is a positive regulator of the activity of sigmaB, the general stress-response sigma factor of Gram+ microorganisms. The N-terminal domain of this protein has no significant sequence homology with proteins of known function, whereas the C-terminal domain is similar to the catalytic domains of PP2C-type phosphatases. The phosphatase activity of RsbU is stimulated greatly during the response to stress by associating with a kinase, RsbT. This association leads to the induction of sigmaB activity. Here we present data on the activation process and demonstrate in vivo that truncations in the N-terminal region of RsbU are deleterious for the activation of RsbU. This conclusion is supported by comparisons of the phosphatase activities of full-length and a truncated form of RsbU in vitro. Our determination of the crystal structure of the N-terminal domain of RsbU from Bacillus subtilis reveals structural similarities to the regulatory domains from ubiquitous protein phosphatases and a conserved domain of sigma-factors, illuminating the activation processes of phosphatases and the evolution of "partner switching." Finally, the molecular basis of kinase recruitment by the RsbU phosphatase is discussed by comparing RsbU sequences from bacteria that either possess or lack RsbT.
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'''KINASE RECRUITMENT DOMAIN OF THE STRESS PHOSPHATASE RSBU'''
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Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C.,Delumeau O, Dutta S, Brigulla M, Kuhnke G, Hardwick SW, Volker U, Yudkin MD, Lewis RJ J Biol Chem. 2004 Sep 24;279(39):40927-37. Epub 2004 Jul 19. PMID:15263010<ref>PMID:15263010</ref>
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==Overview==
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RsbU is a positive regulator of the activity of sigmaB, the general stress-response sigma factor of Gram+ microorganisms. The N-terminal domain of this protein has no significant sequence homology with proteins of known function, whereas the C-terminal domain is similar to the catalytic domains of PP2C-type phosphatases. The phosphatase activity of RsbU is stimulated greatly during the response to stress by associating with a kinase, RsbT. This association leads to the induction of sigmaB activity. Here we present data on the activation process and demonstrate in vivo that truncations in the N-terminal region of RsbU are deleterious for the activation of RsbU. This conclusion is supported by comparisons of the phosphatase activities of full-length and a truncated form of RsbU in vitro. Our determination of the crystal structure of the N-terminal domain of RsbU from Bacillus subtilis reveals structural similarities to the regulatory domains from ubiquitous protein phosphatases and a conserved domain of sigma-factors, illuminating the activation processes of phosphatases and the evolution of "partner switching." Finally, the molecular basis of kinase recruitment by the RsbU phosphatase is discussed by comparing RsbU sequences from bacteria that either possess or lack RsbT.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1W53 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W53 OCA].
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</div>
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<div class="pdbe-citations 1w53" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C., Delumeau O, Dutta S, Brigulla M, Kuhnke G, Hardwick SW, Volker U, Yudkin MD, Lewis RJ, J Biol Chem. 2004 Sep 24;279(39):40927-37. Epub 2004 Jul 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15263010 15263010]
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*[[Phosphoserine phosphatase|Phosphoserine phosphatase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brigulla, M.]]
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[[Category: Brigulla M]]
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[[Category: Delumeau, O.]]
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[[Category: Delumeau O]]
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[[Category: Dutta, S.]]
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[[Category: Dutta S]]
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[[Category: Hardwick, S W.]]
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[[Category: Hardwick SW]]
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[[Category: Kuhnke, G.]]
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[[Category: Kuhnke G]]
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[[Category: Lewis, R J.]]
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[[Category: Lewis RJ]]
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[[Category: Voelker, U.]]
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[[Category: Voelker U]]
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[[Category: Yudkin, M D.]]
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[[Category: Yudkin MD]]
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[[Category: Bacillus]]
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[[Category: Hydrolase]]
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[[Category: Kinase]]
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[[Category: Phosphatase]]
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[[Category: Stress]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:10:21 2008''
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Current revision

Kinase recruitment domain of the stress phosphatase RsbU

PDB ID 1w53

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