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[[Image:1xqe.gif|left|200px]]


{{Structure
==The mechanism of ammonia transport based on the crystal structure of AmtB of E. coli.==
|PDB= 1xqe |SIZE=350|CAPTION= <scene name='initialview01'>1xqe</scene>, resolution 2.10&Aring;
<StructureSection load='1xqe' size='340' side='right'caption='[[1xqe]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene>
<table><tr><td colspan='2'>[[1xqe]] 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=1XQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XQE FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
|GENE=  
<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>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xqe OCA], [https://pdbe.org/1xqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xqe RCSB], [https://www.ebi.ac.uk/pdbsum/1xqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xqe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMTB_ECOLI AMTB_ECOLI] Involved in the uptake of ammonia.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xq/1xqe_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1xqe ConSurf].
<div style="clear:both"></div>


'''The mechanism of ammonia transport based on the crystal structure of AmtB of E. coli.'''
==See Also==
 
*[[Ion channels 3D structures|Ion channels 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1XQE 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=1XQE OCA].
 
==Reference==
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]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berneche, S.]]
[[Category: Berneche S]]
[[Category: Kostrewa, D.]]
[[Category: Kostrewa D]]
[[Category: Li, X D.]]
[[Category: Li X-D]]
[[Category: Winkler, F K.]]
[[Category: Winkler FK]]
[[Category: Zheng, L.]]
[[Category: Zheng L]]
[[Category: ACT]]
[[Category: SO4]]
[[Category: ammonia transport]]
[[Category: open conformation]]
[[Category: wild type]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:13:14 2008''

Latest revision as of 16:36, 13 March 2024

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

Structural highlights

1xqe is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMTB_ECOLI Involved in the uptake of ammonia.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1xqe, resolution 2.10Å

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