5a2h | pdb_00005a2h
Crystal Structure of Arabidopsis thaliana Calmodulin-7
Structural highlights
FunctionCALM7_ARATH 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. Activates MPK8 in vitro.[1] Publication Abstract from PubMedCalmodulin (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. Crystal structure of Arabidopsis thaliana calmodulin7 and insight into its mode of DNA binding.,Kumar S, Mazumder M, Gupta N, Chattopadhyay S, Gourinath S FEBS Lett. 2016 Sep;590(17):3029-39. doi: 10.1002/1873-3468.12349. Epub 2016 Aug , 24. PMID:27500568[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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