Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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Insight into Structural Aspects of Histidine 284 of Daphnia magna Arginine Kinase

  • Rao, Zhili (Division of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University) ;
  • Kim, So Young (Division of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University) ;
  • Li, Xiaotong (Division of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University) ;
  • Kim, Da Som (Division of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University) ;
  • Kim, Yong Ju (Department of Herbal Medicine Resources, College of Environmental and Bioresource Sciences, Jeonbuk National University) ;
  • Park, Jung Hee (Division of Biotechnology, College of Environmental & Bioresources Sciences, Jeonbuk National University)
  • Received : 2020.06.19
  • Accepted : 2020.08.10
  • Published : 2020.09.30
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Abstract

Arginine kinase (AK), a bioenergy-related enzyme, is distributed widely in invertebrates. The role of highly conserved histidines in AKs is still unascertained. In this study, the highly conserved histidine 284 (H284) in AK of Daphnia magna (DmAK) was replaced with alanine to elucidate the role of H284. We examined the alteration of catalytic activity and structural changes of H284A in DmAK. The catalytic activity of H284A was reduced dramatically compared to that in wild type (WT). Thus the crystal structure of H284A displayed several structural changes, including the alteration of D324, a hydrogen-bonding network around H284, and the disruption of π-stacking between the imidazole group of the H284 residue and the adenine ring of ATP. These findings suggest that such alterations might affect a conformational change of the specific loop consisting of G310-V322 at the antiparallel β-sheet region. Thus, we speculated that the H284 residue might play an important role in the conformational change of the specific loop when ATP binds to the substrate-binding site of DmAK.

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References

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