2rrt | pdb_00002rrt

Solution structure of Magnesium-bound form of calmodulin C-domain E104D/E140D mutant

spinqualitylabelsall models 2rrt, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2rrt is a 1 chain structure with sequence from African clawed frog. This structure supersedes the now removed PDB entry 2eqc. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: calm1, calm2 (African clawed frog) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CALM_XENLA] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Calmodulin

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