6KY2

Crystal Structure of Arginine Kinase wild type from Daphnia magna

6KY2 の概要

• エントリーDOI: 10.2210/pdb6ky2/pdb
• 分子名称: Arginine kinase, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: kinase, atp binding protein, arginine binding protein, transferase
• 由来する生物種: Daphnia magna
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40611.81

構造登録者

Park, J.H.,Rao, Z.,Kim, S.Y.,Kim, D.S. (登録日: 2019-09-16, 公開日: 2020-09-16, 最終更新日: 2023-11-22)

主引用文献

Rao, Z.,Kim, S.Y.,Li, X.,Kim, D.S.,Kim, Y.J.,Park, J.H.
Insight into Structural Aspects of Histidine 284 of Daphnia magna Arginine Kinase.
Mol.Cells, 43:784-792, 2020

PubMed 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 (AK) was replaced with alanine to elucidate the role of H284. We examined the alteration of catalytic activity and structural changes of H284A in AK. 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 AK.

PubMed: 32863281
DOI: 10.14348/molcells.2020.0136

実験手法

X-RAY DIFFRACTION (1.87 Å)