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1zcd
From Proteopedia
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| , resolution 3.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | nhaA (Escherichia coli) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the Na+/H+ antiporter NhaA
Overview
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.
About this Structure
1ZCD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH., Hunte C, Screpanti E, Venturi M, Rimon A, Padan E, Michel H, Nature. 2005 Jun 30;435(7046):1197-202. PMID:15988517
Page seeded by OCA on Mon Mar 31 01:33:55 2008
