1xqf

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[[Image:1xqf.jpg|left|200px]]
 
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{{Structure
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==The mechanism of ammonia transport based on the crystal structure of AmtB of E. coli.==
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|PDB= 1xqf |SIZE=350|CAPTION= <scene name='initialview01'>1xqf</scene>, resolution 1.80&Aring;
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<StructureSection load='1xqf' size='340' side='right'caption='[[1xqf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1xqf]] 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=1XQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XQF FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.8&#8491;</td></tr>
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|GENE=
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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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1xqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xqf OCA], [https://pdbe.org/1xqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xqf RCSB], [https://www.ebi.ac.uk/pdbsum/1xqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xqf ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1xqe|1XQE]], [[1u7g|1U7G]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xqf OCA], [http://www.ebi.ac.uk/pdbsum/1xqf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xqf RCSB]</span>
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== Function ==
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}}
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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/xq/1xqf_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=1xqf ConSurf].
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<div style="clear:both"></div>
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'''The mechanism of ammonia transport based on the crystal structure of AmtB of E. coli.'''
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==See Also==
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Ammonium is one of the most important nitrogen sources for bacteria, fungi, and plants, but it is toxic to animals. The ammonium transport proteins (methylamine permeases/ammonium transporters/rhesus) are present in all domains of life; however, functional studies with members of this family have yielded controversial results with respect to the chemical identity (NH(4)(+) or NH(3)) of the transported species. We have solved the structure of wild-type AmtB from Escherichia coli in two crystal forms at 1.8- and 2.1-A resolution, respectively. Substrate transport occurs through a narrow mainly hydrophobic pore located at the center of each monomer of the trimeric AmtB. At the periplasmic entry, a binding site for NH(4)(+) is observed. Two phenylalanine side chains (F107 and F215) block access into the pore from the periplasmic side. Further into the pore, the side chains of two highly conserved histidine residues (H168 and H318) bridged by a H-bond lie adjacent, with their edges pointing into the cavity. These histidine residues may facilitate the deprotonation of an ammonium ion entering the pore. Adiabatic free energy calculations support the hypothesis that an electrostatic barrier between H168 and H318 hinders the permeation of cations but not that of the uncharged NH(3.) The structural data and energetic considerations strongly indicate that the methylamine permeases/ammonium transporters/rhesus proteins are ammonia gas channels. Interestingly, at the cytoplasmic exit of the pore, two different conformational states are observed that might be related to the inactivation mechanism by its regulatory partner.
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==About this Structure==
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1XQF 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=1XQF OCA].
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==Reference==
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The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli., Zheng L, Kostrewa D, Berneche S, Winkler FK, Li XD, Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17090-5. Epub 2004 Nov 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15563598 15563598]
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[[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: Berneche, S.]]
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[[Category: Berneche S]]
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[[Category: Kostrewa, D.]]
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[[Category: Kostrewa D]]
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[[Category: Li, X D.]]
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[[Category: Li X-D]]
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[[Category: Winkler, F K.]]
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[[Category: Winkler FK]]
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[[Category: Zheng, L.]]
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[[Category: Zheng L]]
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[[Category: ammonia transport]]
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[[Category: closed conformation]]
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[[Category: wild type]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:53:11 2008''
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Current revision

The mechanism of ammonia transport based on the crystal structure of AmtB of E. coli.

PDB ID 1xqf

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