Premium
Secondary structure of a calcium binding protein (CaBP) from Entamoeba histolytica
Author(s) -
Sahu Sarata C.,
Bhattacharya A.,
Chary Kandala V.R.,
Govil Girjesh
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01204-1
Subject(s) - entamoeba histolytica , calcium binding protein , ef hand , calmodulin , crystallography , protein secondary structure , chemistry , peptide sequence , nuclear magnetic resonance spectroscopy , stereochemistry , calcium , biochemistry , biology , enzyme , gene , genetics , organic chemistry
A calcium binding protein from Entamoeba histolytica , ( Eh CaBP, 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 1 H, 13 C and 15 N spins in Eh CaBP 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 Eh CaBP resemble them.