ArticleJournal of bioenergetics and biomembranes2013
Crystal structure of shrimp arginine kinase in binary complex with arginine-a molecular view of the phosphagen precursor binding to the enzyme.
Article in Journal of bioenergetics and biomembranes, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
- Conformational Dynamics and Structural Transitions of Arginine Kinase: Implications for Catalysis and Allergen Control.Life (Basel, Switzerland) · 2025Review
- A comprehensive review of arginine kinase proteins: What we need to know?Biochemistry and biophysics reports · 2024Review
- Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Heliyon · 2024Article
- Crystal Structure of H227A Mutant of Arginine Kinase inMolecules (Basel, Switzerland) · 2022Article
- A Novel GlutathioneToxins · 2021Article
- Insight into Structural Aspects of Histidine 284 ofMolecules and cells · 2020Article
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- Article
- Arginine kinase shows nucleoside diphosphate kinase-like activity toward deoxythymidine diphosphate.Journal of bioenergetics and biomembranes · 2016Article
- The substrate-free and -bound crystal structures of the duplicated taurocyamine kinase from the human parasite Schistosoma mansoni.The Journal of biological chemistry · 2015Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Arginine kinase (AK) is a key enzyme for energetic balance in invertebrates. Although AK is a well-studied system that provides fast energy to invertebrates using the phosphagen phospho-arginine, the structural details on the AK-arginine binary complex interaction remain unclear. Herein, we determined two crystal structures of the Pacific whiteleg shrimp (Litopenaeus vannamei) arginine kinase, one in binary complex with arginine (LvAK-Arg) and a ternary transition state analog complex (TSAC). We found that the arginine guanidinium group makes ionic contacts with Glu225, Cys271 and a network of ordered water molecules. On the zwitterionic side of the amino acid, the backbone amide nitrogens of Gly64 and Val65 coordinate the arginine carboxylate. Glu314, one of proposed acid-base catalytic residues, did not interact with arginine in the binary complex. This residue is located in the flexible loop 310-320 that covers the active site and only stabilizes in the LvAK-TSAC. This is the first binary complex crystal structure of a guanidine kinase in complex with the guanidine substrate and could give insights into the nature of the early steps of phosphagen biosynthesis.
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