2npe: Difference between revisions

Revision as of 00:48, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2npe.png

Template:STRUCTURE 2npe

An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductanceAn unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance

Template:ABSTRACT PUBMED 17040913

About this StructureAbout this Structure

2NPE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

An unusual twin-his arrangement in the pore of ammonia channels is essential for substrate conductance., Javelle A, Lupo D, Zheng L, Li XD, Winkler FK, Merrick M, J Biol Chem. 2006 Dec 22;281(51):39492-8. Epub 2006 Oct 12. PMID:17040913

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OCA

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-'''An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance'''
+===An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance===
-==Overview==
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-Amt proteins constitute a class of ubiquitous integral membrane proteins that mediate movement of ammonium across cell membranes. They are homotrimers, in which each subunit contains a narrow pore through which substrate transport occurs. Two conserved histidine residues in the pore have been proposed to be necessary for ammonia conductance. By analyzing 14 engineered polar and non-polar variants of these histidines, in Escherichia coli AmtB, we show that both histidines are absolutely required for optimum substrate conductance. Crystal structures of variants confirm that substitution of the histidine residues does not affect AmtB structure. In a subgroup of Amt proteins, found only in fungi, one of the histidines is replaced by glutamate. The equivalent substitution in E. coli AmtB is partially active, and the structure of this variant suggests that the glutamate side chain can make similar interactions to those made by histidine.
+The line below this paragraph, {{ABSTRACT_PUBMED_17040913}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17040913}}
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 [[Category: Histidine mutant]]
 [[Category: Membrane protein]]
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