7VCJ
Arginine kinase H227A from Daphnia magna
Summary for 7VCJ
| Entry DOI | 10.2210/pdb7vcj/pdb |
| Descriptor | Arginine kinase, PHOSPHATE ION, NITRATE ION, ... (4 entities in total) |
| Functional Keywords | arginine kinase, stability, secondary structure, transferase |
| Biological source | Daphnia magna |
| Total number of polymer chains | 1 |
| Total formula weight | 40535.67 |
| Authors | Kim, D.S.,Jang, K.,Kim, W.S.,Kim, Y.J.,Park, J.H. (deposition date: 2021-09-03, release date: 2022-02-16, Last modification date: 2023-11-29) |
| Primary citation | Kim, D.S.,Jang, K.,Kim, W.S.,Ryu, M.,Park, J.H.,Kim, Y.J. Crystal Structure of H227A Mutant of Arginine Kinase in Daphnia magna Suggests the Importance of Its Stability. Molecules, 27:-, 2022 Cited by PubMed Abstract: Arginine kinase (AK) plays a crucial role in the survival of , a water flea and a common planktonic invertebrate sensitive to water pollution, owing to the production of bioenergy. AK from (AK) has four highly conserved histidine residues, namely, H90, H227, H284, and H315 in the amino acid sequence. In contrast to AK WT (wild type), the enzyme activity of the H227A mutant decreases by 18%. To identify the structure-function relationship of this H227A mutant enzyme, the crystal 3D X-ray structure has been determined and an unfolding assay using anilino-1-naphthalenesulfonic acid (ANS) fluorescence has been undertaken. The results revealed that when compared to the AK WT, the hydrogen bonding between H227 and A135 was broken in the H227A crystal structure. This suggests that H227 residue, closed to the arginine binding site, plays an important role in maintaining the structural stability and maximizing the enzyme activity through hydrogen bonding with the backbone oxygen of A135. PubMed: 35164149DOI: 10.3390/molecules27030884 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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