1zcd: Difference between revisions

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[[Image:1zcd.gif|left|200px]]
{{Seed}}
[[Image:1zcd.png|left|200px]]


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{{STRUCTURE_1zcd|  PDB=1zcd  |  SCENE=  }}  
{{STRUCTURE_1zcd|  PDB=1zcd  |  SCENE=  }}  


'''Crystal structure of the Na+/H+ antiporter NhaA'''
===Crystal structure of the Na+/H+ antiporter NhaA===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15988517}}


==About this Structure==
==About this Structure==
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[[Category: Antiporter]]
[[Category: Antiporter]]
[[Category: Membrane protein]]
[[Category: Membrane protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:27:29 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:22:09 2008''

Revision as of 01:22, 29 July 2008

File:1zcd.png

Template:STRUCTURE 1zcd

Crystal structure of the Na+/H+ antiporter NhaA

Template:ABSTRACT PUBMED 15988517

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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