6ky2
Crystal Structure of Arginine Kinase wild type from Daphnia magnaCrystal Structure of Arginine Kinase wild type from Daphnia magna
Structural highlights
FunctionPublication Abstract from PubMedArginine 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 pi-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 beta-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. Insight into Structural Aspects of Histidine 284 of Daphnia magna Arginine Kinase.,Rao Z, Kim SY, Li X, Kim DS, Kim YJ, Park JH Mol Cells. 2020 Sep 30;43(9):784-792. doi: 10.14348/molcells.2020.0136. PMID:32863281[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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