Crystal structure and trimer-monomer transition of N-terminal domain of EhCaBP1 from Entamoeba histolytica.

ABSTRACT: EhCaBP1 is a well-characterized calcium binding protein from Entamoeba histolytica with four canonical EF-hand motifs. The crystal structure of EhCaBP1 reveals the trimeric organization of N-terminal domain. The solution structure obtained at pH 6.0 indicated its monomeric nature, similar to that of calmodulin. Recent domain-wise studies showed clearly that the N-terminal domain of EhCaBP1 is capable of performing most of the functions of the full-length protein. Additionally, the mode of target binding in the trimer is similar to that found in calmodulin. To study the dynamic nature of this protein and further validate the trimerization of N-terminal domain at physiological conditions, the crystal structure of N-terminal domain was determined at 2.5 A resolution. The final structure consi

SUBMITTER: Kumar S 

PROVIDER: S-EPMC2884261 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature