ArticleThe Journal of biological chemistry2011
The structure of lombricine kinase: implications for phosphagen kinase conformational changes.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Structural Insights into Arginine Kinase and Phosphagen Kinase Homologs: Mechanisms of Catalysis, Regulation, and Evolution.Biology · 2025Review
- Complex structure and activation mechanism of arginine kinase McsB by McsA.Nature chemical biology · 2025Article
- Structural insights into the regulation of protein-arginine kinase McsB by McsA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- Elevated μs-ms timescale backbone dynamics in the transition state analog form of arginine kinase.Journal of structural biology · 2017Article
- The Michaelis Complex of Arginine Kinase Samples the Transition State at a Frequency That Matches the Catalytic Rate.Journal of the American Chemical Society · 2017Article
- Insights into the Phosphoryl Transfer Mechanism of Human Ubiquitous Mitochondrial Creatine Kinase.Scientific reports · 2016Article
- Model of the Ankyrin and SOCS Box Protein, ASB9, E3 Ligase Reveals a Mechanism for Dynamic Ubiquitin Transfer.Structure (London, England : 1993) · 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
- Crystal structure of shrimp arginine kinase in binary complex with arginine-a molecular view of the phosphagen precursor binding to the enzyme.Journal of bioenergetics and biomembranes · 2013Article
- Crystal structures of arginine kinase in complex with ADP, nitrate, and various phosphagen analogs.Biochemical and biophysical research communications · 2012Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
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Abstract
Lombricine kinase is a member of the phosphagen kinase family and a homolog of creatine and arginine kinases, enzymes responsible for buffering cellular ATP levels. Structures of lombricine kinase from the marine worm Urechis caupo were determined by x-ray crystallography. One form was crystallized as a nucleotide complex, and the other was substrate-free. The two structures are similar to each other and more similar to the substrate-free forms of homologs than to the substrate-bound forms of the other phosphagen kinases. Active site specificity loop 309-317, which is disordered in substrate-free structures of homologs and is known from the NMR of arginine kinase to be inherently dynamic, is resolved in both lombricine kinase structures, providing an improved basis for understanding the loop dynamics. Phosphagen kinases undergo a segmented closing on substrate binding, but the lombricine kinase ADP complex is in the open form more typical of substrate-free homologs. Through a comparison with prior complexes of intermediate structure, a correlation was revealed between the overall enzyme conformation and the substrate interactions of His(178). Comparative modeling provides a rationale for the more relaxed specificity of these kinases, of which the natural substrates are among the largest of the phosphagen substrates.
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