View source for 2rrt


==Solution structure of Magnesium-bound form of calmodulin C-domain E104D/E140D mutant==
<StructureSection load='2rrt' size='340' side='right'caption='[[2rrt]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rrt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2eqc 2eqc]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RRT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrt OCA], [https://pdbe.org/2rrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rrt RCSB], [https://www.ebi.ac.uk/pdbsum/2rrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrt ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Calmodulin (CaM) is a Ca(2+)-binding protein that functions as a ubiquitous Ca(2+)-signaling molecule, through conformational changes from the "closed" apo conformation to the "open" Ca(2+)-bound conformation. Mg(2+) also binds to CaM and stabilizes its folded structure, but the NMR signals are broadened by slow conformational fluctuations. Using the E104D/E140D mutant, designed to decrease the signal broadening in the presence of Mg(2+) with minimal perturbations of the overall structure, the solution structure of the Mg(2+)-bound form of the CaM C-terminal domain was determined by multidimensional NMR spectroscopy. The Mg(2+)-induced conformational change mainly occurred in EF hand IV, while EF-hand III retained the apo structure. The helix G and helix H sides of the binding sequence undergo conformational changes needed for the Mg(2+) coordination, and thus the helices tilt slightly. The aromatic rings on helix H move to form a new cluster of aromatic rings in the hydrophobic core. Although helix G tilts slightly to the open orientation, the closed conformation is maintained. The fact that the Mg(2+)-induced conformational changes in EF-hand IV and the hydrophobic core are also seen upon Ca(2+) binding suggests that the Ca(2+)-induced conformational changes can be divided into two categories, those specific to Ca(2+) and those common to Ca(2+) and Mg(2+).

Solution structure and fluctuation of the Mg(2+)-bound form of calmodulin C-terminal domain.,Ohashi W, Hirota H, Yamazaki T Protein Sci. 2011 Apr;20(4):690-701. doi: 10.1002/pro.598. PMID:21312310<ref>PMID:21312310</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 2rrt" style="background-color:#fffaf0;"></div>

==See Also==
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Hirota H]]
[[Category: Ohashi W]]
[[Category: Yamazaki T]]