Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-06

AUTHORS

Carola Hunte, Emanuela Screpanti, Miro Venturi, Abraham Rimon, Etana Padan, Hartmut Michel

ABSTRACT

The control by Na+/H+ antiporters of sodium/proton concentration and cell volume is crucial for the viability of all cells. Adaptation to high salinity and/or extreme pH in plants and bacteria or in human heart muscles requires the action of Na+/H+ antiporters. Their activity is tightly controlled by pH. Here we present the crystal structure of pH-downregulated NhaA, the main antiporter of Escherichia coli and many enterobacteria. A negatively charged ion funnel opens to the cytoplasm and ends in the middle of the membrane at the putative ion-binding site. There, a unique assembly of two pairs of short helices connected by crossed, extended chains creates a balanced electrostatic environment. We propose that the binding of charged substrates causes an electric imbalance, inducing movements, that permit a rapid alternating-access mechanism. This ion-exchange machinery is regulated by a conformational change elicited by a pH signal perceived at the entry to the cytoplasmic funnel. More... »

PAGES

1197-1202

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature03692

DOI

http://dx.doi.org/10.1038/nature03692

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038722325

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15988517


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