2lc5

Calmodulin-like Protein from Entamoeba histolytica: Solution Structure and Calcium-Binding Properties of a Partially Folded ProteinCalmodulin-like Protein from Entamoeba histolytica: Solution Structure and Calcium-Binding Properties of a Partially Folded Protein

Structural highlights 2lc5 is a 1 chain structure with sequence from Entamoeba histolytica HM-1:IMSS. This structure supersedes the now removed PDB entry 2ktg. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C4M0U8_ENTH1 Publication Abstract from PubMed The mechanism of Ca(2+)-signaling in the protozoan parasite Entamoeba histolytica is yet to be understood as many of the key regulators are still to be identified. E. histolytica encodes a number of multi-EF-hand Ca(2+)-binding proteins (EhCaBPs). Functionally only one of these molecules, EhCaBP1, has been characterized to date. The calmodulin-like protein from E. histolytica (abbreviated as EhCaM or EhCaBP3) is a 17.23 kDa monomeric protein that shows maximum sequence identity with heterologous calmodulins (CaMs). Though CaM activity has been biochemically shown in E. histolytica, there are no reports on the presence of a typical CaM. In an attempt to understand the structural and functional similarity of EhCaM with CaM, we have determined the three-dimensional (3D) solution structure of EhCaM using NMR. The EhCaM has a well-folded N-terminal domain and an unstructured C-terminal counterpart. Further, it sequentially binds only two calcium ions, an unusual mode of Ca(2+)-binding among the known CaBPs, notably both in the N-terminal domain of EhCaM. Further, EhCaM is present in the nucleus in addition to the cytoplasm as detected by immunofluorescence staining, unlike other EhCaBPs that are detected only in the cytoplasm. Therefore, this protein is likely to have a different function. The presence of unusual and a diverse set of CaBPs in E. histolytica suggests a distinct Ca(2+)-signaling process in E. histolytica. The results reported here help in understanding the structure-function relationship of CaBPs including their Ca(2+)-binding properties. Calmodulin-like Protein from Entamoeba histolytica: Solution Structure and Calcium-Binding Properties of a Partially Folded Protein.,Rout AK, Padhan N, Barnwal RP, Bhattacharya A, Chary KV Biochemistry. 2010 Dec 21. PMID:21114322 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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