1d5w: Difference between revisions

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OCA

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-[[Image:1d5w.gif|left|200px]]<br /><applet load="1d5w" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1d5w, resolution 2.30&Aring;" />
-'''PHOSPHORYLATED FIXJ RECEIVER DOMAIN'''<br />
-==Overview==
+==PHOSPHORYLATED FIXJ RECEIVER DOMAIN==
-BACKGROUND: A variety of bacterial adaptative cellular responses to, environmental stimuli are mediated by two-component signal transduction, pathways. In these phosphorelay cascades, histidine kinases, transphosphorylate a conserved aspartate in the receiver domain, a, conserved module in the response regulator superfamily. The main effect of, this phosphorylation is to alter the conformation of the response, regulator in order to modulate its biological function. The response, regulator FixJ displays a typical modular arrangement, with a, phosphorylatable N-terminal receiver domain and a C-terminal DNA-binding, domain. In the symbiotic bacterium Sinorhizobium meliloti, phosphorylation, of this response regulator activates transcription of nitrogen-fixation, genes. RESULTS: The crystal structures of the phosphorylated and of the, unphosphorylated N-terminal receiver domain of FixJ (FixJN) were solved at, 2.3 A and 2.4 A resolution, respectively. They reveal the environment of, the phosphoaspartate in the active site and the specific conformational, changes leading to activation of the response regulator. Phosphorylation, of the conserved aspartate induces major structural changes in the beta, 4-alpha 4 loop, and in the signaling surface alpha 4-beta 5 that mediates, dimerization of the phosphorylated full-length response regulator. A, site-directed mutant at this protein-protein interface decreases the, affinity of the phosphorylated response regulator for the fixK promoter, tenfold. CONCLUSIONS: The cascade of phosphorylation-induced, conformational changes in FixJN illustrates the role of conserved residues, in stabilizing the phosphoryl group in the active site, triggering the, structural transition and achieving the post-phosphorylation signaling, events. We propose that these phosphorylation-induced conformational, changes underly the activation of response regulators in general.
+<StructureSection load='1d5w' size='340' side='right'caption='[[1d5w]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1d5w]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D5W FirstGlance]. <br>
-D5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D5W OCA].
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d5w OCA], [https://pdbe.org/1d5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d5w RCSB], [https://www.ebi.ac.uk/pdbsum/1d5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d5w ProSAT]</span></td></tr>
-Conformational changes induced by phosphorylation of the FixJ receiver domain., Birck C, Mourey L, Gouet P, Fabry B, Schumacher J, Rousseau P, Kahn D, Samama JP, Structure. 1999 Dec 15;7(12):1505-15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10647181 10647181]
+</table>
-[[Category: Single protein]]
+== Function ==
+[https://www.uniprot.org/uniprot/FIXJ_RHIME FIXJ_RHIME] FixJ, when activated by FixL, induces the expression of both nifA, required for activation of classical nif and fix genes, and fixK, required for FixN activation.
+== 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/d5/1d5w_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=1d5w ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Sinorhizobium meliloti]]
-[[Category: Birck, C.]]
+[[Category: Birck C]]
-[[Category: Fabry, B.]]
+[[Category: Fabry B]]
-[[Category: Gouet, P.]]
+[[Category: Gouet P]]
-[[Category: Kahn, D.]]
+[[Category: Kahn D]]
-[[Category: Mourey, L.]]
+[[Category: Mourey L]]
-[[Category: Rousseau, P.]]
+[[Category: Rousseau P]]
-[[Category: Samama, J.P.]]
+[[Category: Samama JP]]
-[[Category: Schumacher, J.]]
+[[Category: Schumacher J]]
-[[Category: SO4]]
-[[Category: doubly wound five-stranded beta/alpha fold]]
-[[Category: nitrogen fixation regulation]]
-[[Category: phosphorylated protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:01:48 2007''