4HEX
A novel conformation of calmodulin
Summary for 4HEX
| Entry DOI | 10.2210/pdb4hex/pdb |
| Descriptor | Calmodulin, ZINC ION, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | calmodulin, novel conformation, trans, ef-hand motifs, calcium signalling, calcium binding, neuromodulin, neurogranin, calcium binding protein |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 36178.02 |
| Authors | Kumar, V.,Chichili, V.P.R.,Sivaraman, J. (deposition date: 2012-10-04, release date: 2013-03-06, Last modification date: 2024-03-20) |
| Primary citation | Kumar, V.,Chichili, V.P.R.,Tang, X.,Sivaraman, J. A novel trans conformation of ligand-free calmodulin Plos One, 8:e54834-e54834, 2013 Cited by PubMed Abstract: Calmodulin (CaM) is a highly conserved eukaryotic protein that binds specifically to more than 100 target proteins in response to calcium (Ca(2+)) 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 Ca(2+)/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. PubMed: 23382982DOI: 10.1371/journal.pone.0054834 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.001 Å) |
Structure validation
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