Open AccessCrystallization and preliminary crystallographic analysis of calcium‐binding protein‐2 from Entamoeba histolytica and its complexes with strontium and the IQ1 motif of myosin V
Author(s) -
Alam Neelima,
Padhan Narendra,
Gourinath S.,
Bhattacharya Alok
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105007955
Subject(s) - entamoeba histolytica , crystallization , calcium binding protein , calcium , crystallography , strontium , chemistry , biology , microbiology and biotechnology , organic chemistry
Calcium plays a pivotal role in the pathogenesis of amoebiasis, a major disease caused by Entamoeba histolytica . Two domains with four canonical EF‐hand‐containing calcium‐binding proteins (CaBPs) have been identified from E. histolytica . Even though they have very high sequence similarity, these bind to different target proteins in a Ca 2+ ‐dependent manner, leading to different functional pathways. Calcium‐binding protein‐2 (EhCaBP2) crystals were grown using MPD as a precipitant. The crystals belong to space group P 2 1 , with unit‐cell parameters a = 111.74, b = 68.83, c = 113.25 Å, β = 116.7°. EhCaBP2 also crystallized in complex with strontium (replacing calcium) at similar conditions. The crystals belong to space group P 2 1 , with unit‐cell parameters a = 69.18, b = 112.03, c = 93.42 Å, β = 92.8°. Preliminary data for EhCaBP2 crystals in complex with an IQ motif are also reported. This complex was crystallized with MPD and ethanol as precipitating agents. These crystals belong to space group P 2 1 , with unit‐cell parameters a = 60.5, b = 69.86, c = 86.5 Å, β = 97.9°.