Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0054834
Title: A Novel Trans Conformation of Ligand-Free Calmodulin
Authors: Kumar, V.
Chichili, V.P.R.
Tang, X. 
Sivaraman, J. 
Issue Date: 29-Jan-2013
Citation: Kumar, V., Chichili, V.P.R., Tang, X., Sivaraman, J. (2013-01-29). A Novel Trans Conformation of Ligand-Free Calmodulin. PLoS ONE 8 (1) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0054834
Abstract: Calmodulin (CaM) is a highly conserved eukaryotic protein that binds specifically to more than 100 target proteins in response to calcium (Ca2+) signal. CaM adopts a considerable degree of structural plasticity to accomplish this physiological role; however, the nature and extent of this plasticity remain to be fully understood. Here, we report the crystal structure of a novel trans conformation of ligand-free CaM where the relative disposition of two lobes of CaM is different, a conformation to-date not reported. While no major structural changes were observed in the independent N- and C-lobes as compared with previously reported structures of Ca2+/CaM, the central helix was tilted by ~90° at Arg75. This is the first crystal structure of CaM to show a drastic conformational change in the central helix, and reveals one of several possible conformations of CaM to engage with its binding partner. © 2013 Kumar et al.
Source Title: PLoS ONE
URI: http://scholarbank.nus.edu.sg/handle/10635/113123
ISSN: 19326203
DOI: 10.1371/journal.pone.0054834
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