1zcd

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|ACTIVITY=
|ACTIVITY=
|GENE= nhaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= nhaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zcd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zcd OCA], [http://www.ebi.ac.uk/pdbsum/1zcd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zcd RCSB]</span>
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[[Category: membrane protein]]
[[Category: membrane protein]]
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Revision as of 22:33, 30 March 2008


PDB ID 1zcd

Drag the structure with the mouse to rotate
, 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

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