ArticleBiochemistry2012
X-ray structures of magnesium and manganese complexes with the N-terminal domain of calmodulin: insights into the mechanism and specificity of metal ion binding to an EF-hand.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Molecular basis for a CaThe Journal of biological chemistry · 2026Article
- Redesign of Calmodulin for Genetically Encoded ZnChemical & biomedical imaging · 2026Article
- Selective Identification of Maneb and Mancozeb via MnACS omega · 2026Article
- Increase of Intracellular Zinc Levels Rather Than Zinc Influx Inhibits Interleukin-2 Production in Zinc Supplemented Jurkat Cells.Cell biochemistry and function · 2025Article
- Interaction between the mitochondrial adaptor MIRO and the motor adaptor TRAK.The Journal of biological chemistry · 2023Article
- ADP enhances the allosteric activation of eukaryotic elongation factor 2 kinase by calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Development and characterization of novel jGCaMP8f calcium sensor variants with improved kinetics and fluorescence response range.Frontiers in cellular neuroscience · 2023Article
- A genetically encoded fluorescent sensor for manganese(II), engineered from lanmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- NMR Structures of Calmodulin Bound to Two Separate Regulatory Sites in the Retinal Cyclic Nucleotide-Gated Channel.Biochemistry · 2022Article
- Nanomolar affinity of EF-hands in neuronal calcium sensor 1 for bivalent cations Pb2+, Mn2+, and Hg2.Metallomics : integrated biometal science · 2022Article
- Structural basis for the calmodulin-mediated activation of eukaryotic elongation factor 2 kinase.Science advances · 2022Article
- Chelator-Based Parameterization of the 12-6-4 Lennard-Jones Molecular Mechanics Potential for More Realistic Metal Ion-Protein Interactions.Journal of chemical theory and computation · 2022Article
- Mass Spectrometry-Based Structural Proteomics for Metal Ion/Protein Binding Studies.Biomolecules · 2022Review
- Transport, functions, and interaction of calcium and manganese in plant organellar compartments.Plant physiology · 2021Review
- Physiologically Relevant Free CaJournal of molecular biology · 2021Article
- NMR and EPR-DEER Structure of a Dimeric Guanylate Cyclase Activator Protein-5 from Zebrafish Photoreceptors.Biochemistry · 2021Article
- Structural characterization of the mitochondrial CaiScience · 2021Review
- The essential inner membrane protein YejM is a metalloenzyme.Scientific reports · 2020Article
- The molecular basis for diminished muscle function in acidosis: a proposal.Journal of muscle research and cell motility · 2020Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
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2 authors.
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Abstract
Calmodulin (CaM), a member of the EF-hand superfamily, regulates many aspects of cell function by responding specifically to micromolar concentrations of Ca(2+) in the presence of an ~1000-fold higher concentration of cellular Mg(2+). To explain the structural basis of metal ion binding specificity, we have determined the X-ray structures of the N-terminal domain of calmodulin (N-CaM) in complexes with Mg(2+), Mn(2+), and Zn(2+). In contrast to Ca(2+), which induces domain opening in CaM, octahedrally coordinated Mg(2+) and Mn(2+) stabilize the closed-domain, apo-like conformation, while tetrahedrally coordinated Zn(2+) ions bind at the protein surface and do not compete with Ca(2+). The relative positions of bound Mg(2+) and Mn(2+) within the EF-hand loops are similar to those of Ca(2+); however, the Glu side chain at position 12 of the loop, whose bidentate interaction with Ca(2+) is critical for domain opening, does not bind directly to either Mn(2+) or Mg(2+), and the vacant ligand position is occupied by a water molecule. We conclude that this critical interaction is prevented by specific stereochemical constraints imposed on the ligands by the EF-hand β-scaffold. The structures suggest that Mg(2+) contributes to the switching off of calmodulin activity and possibly other EF-hand proteins at the resting levels of Ca(2+). The Mg(2+)-bound N-CaM structure also provides a unique view of a transiently bound hydrated metal ion and suggests a role for the hydration water in the metal-induced conformational change.
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