Secondary structure of a calcium binding protein (CaBP) from Entamoeba histolytica

FEBS Letters

Sahu, Sarata C.²  Chary, Kandala V.R.²  Bhattacharya, A.¹  Govil, Girjesh² 

[1] School of Life Sciences, Jawaharlal Nehru University, New Mehrauli Road, New Delhi 110 067, India;Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai 400 005, India

关键词: Calcium binding protein;    NMR assignment;    Secondary structure;    EF family;    Entamoeba histolytica;   

DOI  :  10.1016/S0014-5793(99)01204-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A calcium binding protein from Entamoeba histolytica, (EhCaBP, M _r∼15 kDa) is the causative agent for amoebiosis and has a very low sequence homology (∼30%) with other known CaBPs. Almost complete sequence specific resonance assignments for ¹H, ¹³C and ¹⁵N spins in EhCaBP were obtained using double and triple resonance NMR experiments. Qualitative interpretation of the nuclear Overhauser enhancements, chemical shift indices and of hydrogen exchange rates threw valuable light upon the secondary structure of this protein. CaBP is found to have two globular domains each of which consists of two pairs of helix-loop-helix motifs. Though this protein has a very small sequence homology with calmodulins, the topological arrangement of the α-helices and β-strands in EhCaBP resemble them.

【 授权许可】

Unknown