5A2H
Crystal Structure of Arabidopsis thaliana Calmodulin-7
Summary for 5A2H
| Entry DOI | 10.2210/pdb5a2h/pdb |
| Descriptor | CALMODULIN, CALCIUM ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total) |
| Functional Keywords | calcium-binding protein, protein |
| Biological source | ARABIDOPSIS THALIANA (MOUSE-EAR CRESS, THALE-CRESS) |
| Total number of polymer chains | 1 |
| Total formula weight | 17437.51 |
| Authors | Kumar, S.,Gourinath, S. (deposition date: 2015-05-19, release date: 2016-03-30, Last modification date: 2024-01-10) |
| Primary citation | Kumar, S.,Mazumder, M.,Gupta, N.,Chattopadhyay, S.,Gourinath, S. Crystal Structure of Arabidopsis Thaliana Calmodulin7 and Insight Into its Mode of DNA Binding. FEBS Lett., 590:3029-, 2016 Cited by PubMed Abstract: Calmodulin (CaM) is a Ca(2+) sensor that participates in several cellular signaling cascades by interacting with various targets, including DNA. It has been shown that Arabidopsis thaliana CaM7 (AtCaM7) interacts with Z-box DNA and functions as a transcription factor [Kushwaha R et al. (2008) Plant Cell 20, 1747-1759; Abbas N et al. (2014) Plant Cell 26, 1036-1052]. The crystal structure of AtCaM7, and a model of the AtCAM7-Z-box complex suggest that Arg-127 determines the DNA-binding ability by forming crucial interactions with the guanine base. We validated the model using biolayer interferometry, which confirmed that AtCaM7 interacts with Z-box DNA with high affinity. In contrast, the AtCaM2/3/5 isoform does not show any binding, although it differs from AtCaM7 by only a single residue. PubMed: 27500568DOI: 10.1002/1873-3468.12349 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
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