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Insight into Structural Aspects of Histidine 284 of Daphnia magna Arginine Kinase

Molecules and Cells 2020년 43권 9호 p.784 ~ 792
Rao Zhili, 김소영, Li Xiaotong, 김다솜, 김용주, 박정희,
소속 상세정보
 ( Rao Zhili ) - Chonbuk National University College of Environmental and Bioresource Sciences Division of Biotechnology
김소영 ( Kim So-Young ) - Chonbuk National University College of Environmental and Bioresource Sciences Division of Biotechnology
 ( Li Xiaotong ) - Chonbuk National University College of Environmental and Bioresource Sciences Division of Biotechnology
김다솜 ( Kim Da-Som ) - Chonbuk National University College of Environmental and Bioresource Sciences Division of Biotechnology
김용주 ( Kim Yong-Ju ) - Jeonbuk National University College of Environmental and Bioresource Sciences Department of Herbal Medicine Resources
박정희 ( Park Jung-Hee ) - Chonbuk National University College of Environmental and Bioresource Sciences Division of Biotechnology

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.

키워드

arginine kinase; crystallization; kinetics; point mutation; X-ray crystallography

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