Crystallization and preliminary crystallographic analysis of calcium-binding protein-2 from Entamoeba histolytica and its complexes with strontium and the IQ1 motif of myosin V

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Samudrala GourinathAlok Bhattacharya

Abstract

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 Ca2+-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 P2(1), with unit-cell parameters a = 111.74, b = 68.83, c = 113.25 A, beta = 116.7 degrees. EhCaBP2 also crystallized in complex with strontium (replacing calcium) at similar conditions. The crystals belong to space group P2(1), with unit-cell parameters a = 69.18, b = 112.03, c = 93.42 A, beta = 92.8 degrees. 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 P2(1), with unit-cell parameters a = 60.5, b = 69.86, c = 86.5 A, beta = 97.9 degrees.

References

Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Jan 1, 1997·Molecular and Biochemical Parasitology·N YadavaA Bhattacharya
Mar 26, 2002·FEBS Letters·Martin Bähler, Allen Rhoads

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Citations

Nov 30, 2012·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Sanjeev KumarSamudrala Gourinath
May 8, 2020·PLoS Pathogens·Mrigya BabutaAlok Bhattacharya

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