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New page: left|200px<br /><applet load="1g90" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g90" /> '''NMR Solution Structure of Outer Membrane Pro...
 
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[[Image:1g90.gif|left|200px]]<br /><applet load="1g90" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1g90" />
'''NMR Solution Structure of Outer Membrane Protein A Transmembrane Domain: 10 conformers'''<br />


==Overview==
==NMR Solution Structure of Outer Membrane Protein A Transmembrane Domain: 10 conformers==
We have determined the three-dimensional fold of the 19 kDa (177 residues), transmembrane domain of the outer membrane protein A of Escherichia coli, in dodecylphosphocholine (DPC) micelles in solution using heteronuclear, NMR. The structure consists of an eight-stranded beta-barrel connected by, tight turns on the periplasmic side and larger mobile loops on the, extracellular side. The solution structure of the barrel in DPC micelles, is similar to that in n-octyltetraoxyethylene (C(8)E(4)) micelles, determined by X-ray diffraction. Moreover, data from NMR dynamic, experiments reveal a gradient of conformational flexibility in the, structure that may contribute to the membrane channel function of this, protein.
<StructureSection load='1g90' size='340' side='right'caption='[[1g90]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1g90]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G90 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1g90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g90 OCA], [https://pdbe.org/1g90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g90 RCSB], [https://www.ebi.ac.uk/pdbsum/1g90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g90 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OMPA_ECOLI OMPA_ECOLI] Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes.
== 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/g9/1g90_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=1g90 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have determined the three-dimensional fold of the 19 kDa (177 residues) transmembrane domain of the outer membrane protein A of Escherichia coli in dodecylphosphocholine (DPC) micelles in solution using heteronuclear NMR. The structure consists of an eight-stranded beta-barrel connected by tight turns on the periplasmic side and larger mobile loops on the extracellular side. The solution structure of the barrel in DPC micelles is similar to that in n-octyltetraoxyethylene (C(8)E(4)) micelles determined by X-ray diffraction. Moreover, data from NMR dynamic experiments reveal a gradient of conformational flexibility in the structure that may contribute to the membrane channel function of this protein.


==About this Structure==
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy.,Arora A, Abildgaard F, Bushweller JH, Tamm LK Nat Struct Biol. 2001 Apr;8(4):334-8. PMID:11276254<ref>PMID:11276254</ref>
1G90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G90 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy., Arora A, Abildgaard F, Bushweller JH, Tamm LK, Nat Struct Biol. 2001 Apr;8(4):334-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11276254 11276254]
</div>
<div class="pdbe-citations 1g90" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Porin 3D structures|Porin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Abildgaard, F.]]
[[Category: Abildgaard F]]
[[Category: Arora, A.]]
[[Category: Arora A]]
[[Category: Bushweller, J.H.]]
[[Category: Bushweller JH]]
[[Category: Tamm, L.K.]]
[[Category: Tamm LK]]
[[Category: beta barrel]]
[[Category: integral membrane protein]]
[[Category: nmr]]
 
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Retrieved from "https://proteopedia.org/1g90"