2nop

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[[Image:2nop.gif|left|200px]]
 
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==An unusual twin-His arrangement in the pore of ammonia channels is essential for substrate conductance==
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The line below this paragraph, containing "STRUCTURE_2nop", creates the "Structure Box" on the page.
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<StructureSection load='2nop' size='340' side='right'caption='[[2nop]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2nop]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NOP FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2nop| PDB=2nop | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nop OCA], [https://pdbe.org/2nop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nop RCSB], [https://www.ebi.ac.uk/pdbsum/2nop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nop ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMTB_ECOLI AMTB_ECOLI] Involved in the uptake of ammonia.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/no/2nop_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nop ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''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.,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<ref>PMID:17040913</ref>
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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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2NOP 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=2NOP OCA].
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</div>
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<div class="pdbe-citations 2nop" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17040913 17040913]
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Lupo, D.]]
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[[Category: Lupo D]]
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[[Category: Winkler, F K.]]
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[[Category: Winkler FK]]
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[[Category: Ammonia transport]]
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[[Category: Membrane protein]]
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[[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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Current revision

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

PDB ID 2nop

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