6KY2
Crystal Structure of Arginine Kinase wild type from Daphnia magna
Summary for 6KY2
| Entry DOI | 10.2210/pdb6ky2/pdb |
| Descriptor | Arginine kinase, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | kinase, atp binding protein, arginine binding protein, transferase |
| Biological source | Daphnia magna |
| Total number of polymer chains | 1 |
| Total formula weight | 40611.81 |
| Authors | Park, J.H.,Rao, Z.,Kim, S.Y.,Kim, D.S. (deposition date: 2019-09-16, release date: 2020-09-16, Last modification date: 2023-11-22) |
| Primary citation | 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 Cited by 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: 32863281DOI: 10.14348/molcells.2020.0136 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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