2ksz

<StructureSection load='2ksz' size='340' side='right'caption='[[2ksz]], [[NMR_Ensembles_of_Models | 5 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2ksz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KSZ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2roa|2roa]], [[1f70|1f70]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SCaM-4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine hispida])</td></tr>

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== Publication Abstract from PubMed ==

Soybean calmodulin isoform 4 (sCaM4) is a plant calcium binding protein, regulating cellular responses to the second messenger Ca(2+). We have found that the metal ion free (apo-) form of sCaM4 possesses a half unfolded structure, with the N-terminal domain unfolded and the C-terminal domain folded. This result was unexpected as the apo-forms of both soybean calmodulin isoform 1 (sCaM1) and mammalian CaM (mCaM) are fully folded. Due to the fact that free Mg(2+) ions are always present at high concentrations in cells (0.5 approximately 2 mM), we suggest that Mg(2+) should be bound to sCaM4 in non-activated cells. CD studies revealed that in the presence of Mg(2+) the initially unfolded N-terminal domain of sCaM4 folds into an alpha-helix-rich structure, similar to the Ca(2+)-form. We have used the NMR backbone residual dipolar coupling (RDC) restraints (1)D(NH), (1)D(CalphaHalpha), and (1)D(C)'(Calpha) to determine the solution structure of the N-terminal domain of Mg(2+)-sCaM4 (Mg(2+)-sCaM4-NT). Compared with the known structure of Ca(2+)-sCaM4, the structure of the Mg(2+)-sCaM4-NT does not fully open the hydrophobic pocket, which was further confirmed by the use of the fluorescent probe ANS. Tryptophan fluorescence experiments were used to study the interactions between Mg(2+)-sCaM4 and CaM-binding peptides derived from smooth muscle myosin light chain kinase as well as plant glutamate decarboxylase. These results suggest that Mg(2+)-sCaM4 does not bind to Ca(2+)-CaM target peptides, and therefore is functionally similar to apo-mCaM. The Mg(2+)- and apo- structures of the sCaM4-NT provide unique insights into the structure and function of some plant calmodulins in resting cells.

The solution structure of the Mg(2+)- form of soybean calmodulin isoform 4 reveals unique features of plant calmodulins in resting cells.,Huang H, Ishida H, Vogel HJ Protein Sci. 2010 Jan 6. PMID:20054830<ref>PMID:20054830</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2ksz" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Glycine hispida]]

[[Category: Huang, H]]

[[Category: Ishida, H]]

[[Category: Vogel, H J]]

[[Category: Soybean calmodulin isoform 4]]