ArticleScientific reports2016
Asymmetric Preorganization of Inverted Pair Residues in the Sodium-Calcium Exchanger.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Article
- Structural insights into epitope-paratope interactions of a monoclonal antibody targeting CEACAM5-expressing tumors.Nature communications · 2024Article
- Inhibition of forward and reverse transport of CaBiological research · 2024Article
- Article
- Conformational free-energy landscapes of a NaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural dynamics of NaCommunications biology · 2024Article
- Na+/Ca2+ exchange in enamel cells is dominated by the K+-dependent NCKX exchanger.The Journal of general physiology · 2024Article
- Structure-Based Function and Regulation of NCX Variants: Updates and Challenges.International journal of molecular sciences · 2022Review
- Exploring the LiCell calcium · 2022Article
- Integrative Study of the Structural and Dynamical Properties of a KirBac3.1 Mutant: Functional Implication of a Highly Conserved Tryptophan in the Transmembrane Domain.International journal of molecular sciences · 2021Article
- New Insights into the Structure-Activity Relationship and Neuroprotective Profile of Benzodiazepinone Derivatives ofJournal of medicinal chemistry · 2021Article
- Proton-modulated interactions of ions with transport sites of prokaryotic and eukaryotic NCX prototypes.Cell calcium · 2021Article
- The leucine zipper EF-hand containing transmembrane protein-1 EF-hand is a tripartite calcium, temperature, and pH sensor.Protein science : a publication of the Protein Society · 2021Article
- The Archaeal NaFrontiers in chemistry · 2021Review
- Interpretation of HDX Data by Maximum-Entropy Reweighting of Simulated Structural Ensembles.Biophysical journal · 2020Article
- Hydrogen-Deuterium Exchange Mass-Spectrometry of Secondary Active Transporters: From Structural Dynamics to Molecular Mechanisms.Frontiers in pharmacology · 2020Review
- Key residues controlling bidirectional ion movements in NaCell calcium · 2018Article
- Article
- Dynamic distinctions in the NaThe Journal of biological chemistry · 2017Article
- Back-exchange of deuterium in neutron crystallography: characterization by IR spectroscopy.Journal of applied crystallography · 2017Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In analogy with many other proteins, Na(+)/Ca(2+) exchangers (NCX) adapt an inverted twofold symmetry of repeated structural elements, while exhibiting a functional asymmetry by stabilizing an outward-facing conformation. Here, structure-based mutant analyses of the Methanococcus jannaschii Na(+)/Ca(2+) exchanger (NCX_Mj) were performed in conjunction with HDX-MS (hydrogen/deuterium exchange mass spectrometry) to identify the structure-dynamic determinants of functional asymmetry. HDX-MS identified hallmark differences in backbone dynamics at ion-coordinating residues of apo-NCX_Mj, whereas Na(+)or Ca(2+) binding to the respective sites induced relatively small, but specific, changes in backbone dynamics. Mutant analysis identified ion-coordinating residues affecting the catalytic capacity (kcat/Km), but not the stability of the outward-facing conformation. In contrast, distinct "noncatalytic" residues (adjacent to the ion-coordinating residues) control the stability of the outward-facing conformation, but not the catalytic capacity. The helix-breaking signature sequences (GTSLPE) on the α1 and α2 repeats (at the ion-binding core) differ in their folding/unfolding dynamics, while providing asymmetric contributions to transport activities. The present data strongly support the idea that asymmetric preorganization of the ligand-free ion-pocket predefines catalytic reorganization of ion-bound residues, where secondary interactions with adjacent residues couple the alternating access. These findings provide a structure-dynamic basis for ion-coupled alternating access in NCX and similar proteins.
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