1u7c: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px<br /><applet load="1u7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u7c, resolution 1.85Å" /> '''Crystal Structure of... |
No edit summary |
||
| (18 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Crystal Structure of AmtB from E.Coli with Methyl Ammonium.== | ||
The first structure of an ammonia channel from the Amt/MEP/Rh protein | <StructureSection load='1u7c' size='340' side='right'caption='[[1u7c]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1u7c]] 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=1U7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U7C FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NME:METHYLAMINE'>NME</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=1u7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u7c OCA], [https://pdbe.org/1u7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u7c RCSB], [https://www.ebi.ac.uk/pdbsum/1u7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u7c 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/u7/1u7c_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=1u7c ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times. Two structurally similar halves span the membrane with opposite polarity. Structures with and without ammonia or methyl ammonia show a vestibule that recruits NH4+/NH3, a binding site for NH4+, and a 20 angstrom-long hydrophobic channel that lowers the NH4+ pKa to below 6 and conducts NH3. Favorable interactions for NH3 are seen within the channel and use conserved histidines. Reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH3. | |||
Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A.,Khademi S, O'Connell J 3rd, Remis J, Robles-Colmenares Y, Miercke LJ, Stroud RM Science. 2004 Sep 10;305(5690):1587-94. PMID:15361618<ref>PMID:15361618</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1u7c" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Khademi S]] | ||
[[Category: | [[Category: Miercke LJW]] | ||
[[Category: | [[Category: O'Connell III J]] | ||
[[Category: Remis | [[Category: Remis J]] | ||
[[Category: Robles-Colmenares | [[Category: Robles-Colmenares Y]] | ||
[[Category: Stroud | [[Category: Stroud RM]] | ||
Latest revision as of 09:39, 23 August 2023
Crystal Structure of AmtB from E.Coli with Methyl Ammonium.Crystal Structure of AmtB from E.Coli with Methyl Ammonium.
Structural highlights
FunctionAMTB_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. Publication Abstract from PubMedThe first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times. Two structurally similar halves span the membrane with opposite polarity. Structures with and without ammonia or methyl ammonia show a vestibule that recruits NH4+/NH3, a binding site for NH4+, and a 20 angstrom-long hydrophobic channel that lowers the NH4+ pKa to below 6 and conducts NH3. Favorable interactions for NH3 are seen within the channel and use conserved histidines. Reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH3. Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A.,Khademi S, O'Connell J 3rd, Remis J, Robles-Colmenares Y, Miercke LJ, Stroud RM Science. 2004 Sep 10;305(5690):1587-94. PMID:15361618[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||