2npk
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An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance
OverviewOverview
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.
About this StructureAbout this Structure
2NPK is a Single protein structure of sequence from Escherichia coli with SO4, ACT, IMD and GOL as ligands. 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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