ArticlePloS one2011
New structural and functional contexts of the Dx[DN]xDG linear motif: insights into evolution of calcium-binding proteins.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 57 citations in OpenAlex.
- Enhanced secretion through type 1 secretion system by grafting a calcium-binding sequence to modify the folding of cargo proteins.Protein science : a publication of the Protein Society · 2025Article
- Why is binding of a divalent metal cation to a structural motif containing four carboxylate residues not accompanied by a conformational change?Protein science : a publication of the Protein Society · 2024Article
- Unveiling the Secrets of Calcium-Dependent Proteins in Plant Growth-Promoting Rhizobacteria: An Abundance of Discoveries Awaits.Plants (Basel, Switzerland) · 2023Review
- Elucidating the Role of a Calcium-Binding Loop in anACS omega · 2023Article
- Auto- and Hetero-Catalytic Processing of the N-Terminal Propeptide Promotes the C-Terminal Fibronectin Type III Domain-Mediated Dimerization of a Thermostable Vpr-like Protease.Applied and environmental microbiology · 2022Article
- Exonic splicing code and protein binding sites for calcium.Nucleic acids research · 2022Article
- New β-Propellers Are Continuously Amplified From Single Blades in all Major Lineages of the β-Propeller Superfamily.Frontiers in molecular biosciences · 2022Article
- How do I get the most out of my protein sequence using bioinformatics tools?Acta crystallographica. Section D, Structural biology · 2021Article
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- The 1.9 Å crystal structure of the extracellular matrix protein Bap1 fromThe Journal of biological chemistry · 2019Article
- Structural characterization of a prolyl aminodipeptidase (PepX) from Lactobacillus helveticus.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Design of a Protein Motif Responsive to Tyrosine Nitration and an Encoded Turn-Off Sensor of Tyrosine Nitration.Biochemistry · 2019Article
- Phosphorylation-dependent protein design: design of a minimal protein kinase-inducible domain.Organic & biomolecular chemistry · 2019Article
- Enhanced calcium carbonate-biofilm complex formation by alkali-generating Lysinibacillus boronitolerans YS11 and alkaliphilic Bacillus sp. AK13.AMB Express · 2019Article
- Redox-Responsive Protein Design: Design of a Small Protein Motif Dependent on Glutathionylation.Biochemistry · 2018Article
- Four Inserts within the Catalytic Domain Confer Extra Stability and Activity to Hyperthermostable Pyrolysin from Pyrococcus furiosus.Applied and environmental microbiology · 2017Article
- Release of an HtrA-Like Protease from the Cell Surface of ThermophilicFrontiers in microbiology · 2017Article
- A Rice Ca2+ Binding Protein Is Required for Tapetum Function and Pollen Formation.Plant physiology · 2016Article
- Ca2+ Regulation of Trypanosoma brucei Phosphoinositide Phospholipase C.Eukaryotic cell · 2015Article
- Extracellular calcium triggers unique transcriptional programs and modulates staurosporine-induced cell death inMicrobial cell (Graz, Austria) · 2014Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Binding of calcium ions (Ca²⁺) to proteins can have profound effects on their structure and function. Common roles of calcium binding include structure stabilization and regulation of activity. It is known that diverse families--EF-hands being one of at least twelve--use a Dx[DN]xDG linear motif to bind calcium in near-identical fashion. Here, four novel structural contexts for the motif are described. Existing experimental data for one of them, a thermophilic archaeal subtilisin, demonstrate for the first time a role for Dx[DN]xDG-bound calcium in protein folding. An integrin-like embedding of the motif in the blade of a β-propeller fold--here named the calcium blade--is discovered in structures of bacterial and fungal proteins. Furthermore, sensitive database searches suggest a common origin for the calcium blade in β-propeller structures of different sizes and a pan-kingdom distribution of these proteins. Factors favouring the multiple convergent evolution of the motif appear to include its general Asp-richness, the regular spacing of the Asp residues and the fact that change of Asp into Gly and vice versa can occur though a single nucleotide change. Among the known structural contexts for the Dx[DN]xDG motif, only the calcium blade and the EF-hand are currently found intracellularly in large numbers, perhaps because the higher extracellular concentration of Ca²⁺ allows for easier fixing of newly evolved motifs that have acquired useful functions. The analysis presented here will inform ongoing efforts toward prediction of similar calcium-binding motifs from sequence information alone.
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