Deepshikha Verma, Shalini Agarwal, Vimal Keerthi, Aruna Murmu, Samudrala Gourinath, Alok Bhattacharya, KandalaV R Chary
Biochemical and biophysical research communications 2020 Jun 30GTPases are molecular switches, which regulate a variety of cellular processes such as cell polarity, gene transcription, microtubule dynamics, cell-cycle etc. In this paper, we characterize a Ca2+-binding protein from Entamoeba histolytica (EhCaBP6) as a novel GTPase. We locate the active site for GTP hydrolysis within the C-terminal domain of EhCaBP6, although it requires full length protein for its complete range of activity. Using NMR studies, we observe that GTP binding induces conformational change in EhCaBP6. The identification of this novel and unusual Ca2+-dependent GTPase is important to elucidate the unconventional cell cycle of E. histolytica. Copyright © 2020 Elsevier Inc. All rights reserved.
Deepshikha Verma, Shalini Agarwal, Vimal Keerthi, Aruna Murmu, Samudrala Gourinath, Alok Bhattacharya, KandalaV R Chary. Ca2+-binding protein from Entamoeba histolytica (EhCaBP6) is a novel GTPase. Biochemical and biophysical research communications. 2020 Jun 30;527(3):631-637
PMID: 32423808
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