1zcd: Difference between revisions
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[[Image:1zcd.gif|left|200px]] | [[Image:1zcd.gif|left|200px]] | ||
'''Crystal structure of the Na+/H+ antiporter NhaA''' | {{Structure | ||
|PDB= 1zcd |SIZE=350|CAPTION= <scene name='initialview01'>1zcd</scene>, resolution 3.45Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= nhaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal structure of the Na+/H+ antiporter NhaA''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZCD is a [ | 1ZCD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZCD OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15988517 15988517] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: membrane protein]] | [[Category: membrane protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:33:45 2008'' | ||
Revision as of 13:33, 20 March 2008
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| 1zcd, resolution 3.45Å | |||||||||||||
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| Gene: | nhaA (Escherichia coli) | ||||||||||||
| 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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