1v1f

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[[Image:1v1f.gif|left|200px]]<br />
 
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<applet load="1v1f" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1v1f, resolution 3.00&Aring;" />
 
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'''STRUCTURE OF THE ARABIDOPSIS THALIANA SOS3 COMPLEXED WITH CALCIUM(II) AND MANGANESE(II) IONS'''<br />
 
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==Overview==
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==Structure of the Arabidopsis thaliana SOS3 complexed with Calcium(II) and Manganese(II) ions==
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The Arabidopsis thaliana SOS3 gene encodes a calcium sensor that is, required for plant salt tolerance. The SOS3 protein binds to and activates, the self-inhibited SOS2 protein kinase, which mediates the expression and, activities of various transporters important for ion homeostasis under, salt stress. SOS3 belongs to a unique family of calcium-binding proteins, that contain two pairs of EF hand motifs with four putative metal-binding, sites. We report the crystal structure of a dimeric SOS3 protein in, complex with calcium, and with calcium and manganese. Analytical, ultracentrifugation experiments and circular dichroism measurements show, that calcium binding is responsible for the dimerization of SOS3. This, leads to a change in the global shape and surface properties of the, protein that may be sufficient to transmit the Ca(2+) signal elicited, during salt stress.
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<StructureSection load='1v1f' size='340' side='right'caption='[[1v1f]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1v1f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V1F FirstGlance]. <br>
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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]] 3&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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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=1v1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v1f OCA], [https://pdbe.org/1v1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v1f RCSB], [https://www.ebi.ac.uk/pdbsum/1v1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v1f ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CNBL4_ARATH CNBL4_ARATH] Acts as a calcium sensor involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Operates in synergy with CIPK24/SOS2 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. May function as positive regulator of salt stress responses. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner.<ref>PMID:11006339</ref> <ref>PMID:10725350</ref> <ref>PMID:12034882</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/v1/1v1f_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=1v1f 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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The Arabidopsis thaliana SOS3 gene encodes a calcium sensor that is required for plant salt tolerance. The SOS3 protein binds to and activates the self-inhibited SOS2 protein kinase, which mediates the expression and activities of various transporters important for ion homeostasis under salt stress. SOS3 belongs to a unique family of calcium-binding proteins that contain two pairs of EF hand motifs with four putative metal-binding sites. We report the crystal structure of a dimeric SOS3 protein in complex with calcium, and with calcium and manganese. Analytical ultracentrifugation experiments and circular dichroism measurements show that calcium binding is responsible for the dimerization of SOS3. This leads to a change in the global shape and surface properties of the protein that may be sufficient to transmit the Ca(2+) signal elicited during salt stress.
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==About this Structure==
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The structure of the Arabidopsis thaliana SOS3: molecular mechanism of sensing calcium for salt stress response.,Sanchez-Barrena MJ, Martinez-Ripoll M, Zhu JK, Albert A J Mol Biol. 2005 Feb 4;345(5):1253-64. Epub 2004 Dec 8. PMID:15644219<ref>PMID:15644219</ref>
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1V1F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with CA, MN, IOD and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: EF1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V1F OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The structure of the Arabidopsis thaliana SOS3: molecular mechanism of sensing calcium for salt stress response., Sanchez-Barrena MJ, Martinez-Ripoll M, Zhu JK, Albert A, J Mol Biol. 2005 Feb 4;345(5):1253-64. Epub 2004 Dec 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15644219 15644219]
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</div>
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<div class="pdbe-citations 1v1f" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Albert, A.]]
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[[Category: Albert A]]
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[[Category: Martinez-Ripoll, M.]]
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[[Category: Martinez-Ripoll M]]
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[[Category: Sanchez-Barrena, M.J.]]
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[[Category: Sanchez-Barrena MJ]]
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[[Category: Zhu, J.K.]]
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[[Category: Zhu JK]]
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[[Category: CA]]
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[[Category: IOD]]
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[[Category: MN]]
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[[Category: MPD]]
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[[Category: calcineurin b-like protein]]
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[[Category: calcium sensor]]
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[[Category: ef-hand]]
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[[Category: protein crystallography]]
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[[Category: salt stress response in plants]]
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[[Category: signalling protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:18:47 2007''
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Current revision

Structure of the Arabidopsis thaliana SOS3 complexed with Calcium(II) and Manganese(II) ions

PDB ID 1v1f

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