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New page: left|200px<br /><applet load="1dck" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dck, resolution 2.00Å" /> '''STRUCTURE OF UNPHOSP...
 
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[[Image:1dck.gif|left|200px]]<br /><applet load="1dck" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dck, resolution 2.00&Aring;" />
'''STRUCTURE OF UNPHOSPHORYLATED FIXJ-N COMPLEXED WITH MN2+'''<br />


==Overview==
==STRUCTURE OF UNPHOSPHORYLATED FIXJ-N COMPLEXED WITH MN2+==
BACKGROUND: Two-component signal transduction pathways are sophisticated, phosphorelay cascades widespread in prokaryotes and also found in fungi, molds and plants. FixL/FixJ is a prototypical system responsible for the, regulation of nitrogen fixation in the symbiotic bacterium Sinorhizobium, meliloti. In microaerobic conditions the membrane-bound kinase FixL uses, ATP to transphosphorylate a histidine residue, and the response regulator, FixJ transfers the phosphoryl group from the phosphohistidine to one of, its own aspartate residues in a Mg(2+)-dependent mechanism. RESULTS: Seven, X-ray structures of the unphosphorylated N-terminal receiver domain of, FixJ (FixJN) have been solved from two crystal forms soaked in different, conditions. Three conformations of the protein were found. In the first, case, the protein fold impairs metal binding in the active site and the, structure reveals a receiver domain that is self-inhibited for catalysis., In the second conformation, the canonical geometry of the active site is, attained, and subsequent metal binding to the protein induces minimal, conformational changes. The third conformation illustrates a non-catalytic, form of the protein where unwinding of the N terminus of helix alpha 1 has, occurred. Interconversion of the canonical and self-inhibited, conformations requires a large conformational change of the beta 3-alpha 3, loop region. CONCLUSIONS: These unphosphorylated structures of FixJN, stress the importance of flexible peptide segments that delineate the, active site. Their movements may act as molecular switches that define the, functional status of the protein. Such observations are in line with, structural and biochemical results obtained on other response regulator, proteins and may illustrate general features that account for the, specificity of protein-protein interactions.
<StructureSection load='1dck' size='340' side='right'caption='[[1dck]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1dck]] is a 2 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=1DCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCK FirstGlance]. <br>
1DCK 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 MN and 15P as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DCK 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&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1dck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dck OCA], [https://pdbe.org/1dck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dck RCSB], [https://www.ebi.ac.uk/pdbsum/1dck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dck ProSAT]</span></td></tr>
Structural transitions in the FixJ receiver domain., Gouet P, Fabry B, Guillet V, Birck C, Mourey L, Kahn D, Samama JP, Structure. 1999 Dec 15;7(12):1517-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10647182 10647182]
</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/dc/1dck_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=1dck ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sinorhizobium meliloti]]
[[Category: Sinorhizobium meliloti]]
[[Category: Birck, C.]]
[[Category: Birck C]]
[[Category: Fabry, B.]]
[[Category: Fabry B]]
[[Category: Gouet, P.]]
[[Category: Gouet P]]
[[Category: Guillet, V.]]
[[Category: Guillet V]]
[[Category: Kahn, D.]]
[[Category: Kahn D]]
[[Category: Mourey, L.]]
[[Category: Mourey L]]
[[Category: Samama, J.P.]]
[[Category: Samama JP]]
[[Category: 15P]]
[[Category: MN]]
[[Category: doubly wound five-stranded beta/alpha fold]]
[[Category: nitrogen fixation regulation]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:10:18 2007''

Latest revision as of 06:52, 7 February 2024

STRUCTURE OF UNPHOSPHORYLATED FIXJ-N COMPLEXED WITH MN2+

1dck, resolution 2.00Å

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