ArticleProceedings of the National Academy of Sciences of the United States of America2015
NhaA antiporter functions using 10 helices, and an additional 2 contribute to assembly/stability.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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.
- Prokaryotic NaInternational journal of molecular sciences · 2022Review
- Insight into the direct interaction of NaScientific reports · 2021Article
- Mechanism of TonB-dependent transport system in Halomonas alkalicola CICC 11012s in response to alkaline stress.Extremophiles : life under extreme conditions · 2021Article
- Continuous Constant pH Molecular Dynamics Simulations of Transmembrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Ion Binding and Selectivity of the NaThe journal of physical chemistry. B · 2020Article
- Cardiolipin is an Optimal Phospholipid for the Assembly, Stability, and Proper Functionality of the Dimeric Form of NhaA NaScientific reports · 2019Article
- Structural and Functional Changes in the NaInternational journal of molecular sciences · 2019Review
- Ligand-induced conformational dynamics of theProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Integrating mass spectrometry with MD simulations reveals the role of lipids in NaNature communications · 2017Article
- Expression and characterization of the SOS1 Arabidopsis salt tolerance protein.Molecular and cellular biochemistry · 2016Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli Na(+)/H(+) antiporter (Ec-NhaA) is the best-characterized of all pH-regulated Na(+)/H(+) exchangers that control cellular Na(+) and H(+) homeostasis. Ec-NhaA has 12 helices, 2 of which (VI and VII) are absent from other antiporters that share the Ec-NhaA structural fold. This α-hairpin is located in the dimer interface of the Ec-NhaA homodimer together with a β-sheet. Here we examine computationally and experimentally the role of the α-hairpin in the stability, dimerization, transport, and pH regulation of Ec-NhaA. Evolutionary analysis (ConSurf) indicates that the VI-VII helical hairpin is much less conserved than the remaining transmembrane region. Moreover, normal mode analysis also shows that intact NhaA and a variant, deleted of the α-hairpin, share similar dynamics, suggesting that the structure may be dispensable. Thus, two truncated Ec-NhaA mutants were constructed, one deleted of the α-hairpin and another also lacking the β-sheet. The mutants were studied at physiological pH in the membrane and in detergent micelles. The findings demonstrate that the truncated mutants retain significant activity and regulatory properties but are defective in the assembly/stability of the Ec-NhaA dimer.
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