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2nop

From Proteopedia

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[[Image:2nop.gif|left|200px]]
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{{Seed}}
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[[Image:2nop.png|left|200px]]
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{{STRUCTURE_2nop| PDB=2nop | SCENE= }}
{{STRUCTURE_2nop| PDB=2nop | SCENE= }}
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'''An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance'''
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===An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance===
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==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.
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The line below this paragraph, {{ABSTRACT_PUBMED_17040913}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 17040913 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17040913}}
==About this Structure==
==About this Structure==
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[[Category: Membrane protein]]
[[Category: Membrane protein]]
[[Category: Wild-type amtb]]
[[Category: Wild-type amtb]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:42:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:15:18 2008''

Revision as of 00:15, 28 July 2008

Image:2nop.png

Template:STRUCTURE 2nop

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

Template:ABSTRACT PUBMED 17040913

About this Structure

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

Reference

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

Page seeded by OCA on Mon Jul 28 03:15:18 2008

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