2LC5

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

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2LC5 の概要

• エントリーDOI: 10.2210/pdb2lc5/pdb
• NMR情報: BMRB: 15663
• 分子名称: Calmodulin, putative, CALCIUM ION (2 entities in total)
• 機能のキーワード: ehcam, ca-binding protein, entamoeba histolytica, partially structured protein, cam-like, metal binding protein
• 由来する生物種: Entamoeba histolytica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17337.43

構造登録者

Rout, A.K.,Padhan, N.,Barnwal, R.P.,Bhattacharya, A.,Chary, K.V. (登録日: 2011-04-23, 公開日: 2011-06-08, 最終更新日: 2024-05-01)

主引用文献

Rout, A.K.,Padhan, N.,Barnwal, R.P.,Bhattacharya, A.,Chary, K.V.
Calmodulin like protein from Entamoeba histolytica: solution structure and calcium binding properties of a partially folded protein.
Biochemistry, 50:181-193, 2010

PubMed Abstract: 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.

PubMed: 21114322
DOI: 10.1021/bi101411q

実験手法

SOLUTION NMR