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[[Image:1bxw.gif|left|200px]]
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{{STRUCTURE_1bxw|  PDB=1bxw  |  SCENE=  }}
'''OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN'''


==OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN==
<StructureSection load='1bxw' size='340' side='right'caption='[[1bxw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bxw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BXW 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</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=1bxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bxw OCA], [https://pdbe.org/1bxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bxw RCSB], [https://www.ebi.ac.uk/pdbsum/1bxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bxw 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/bx/1bxw_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=1bxw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The outer membrane protein A of Escherichia coli (OmpA) is an intensely studied example in the field of membrane protein folding. We have determined the structure of the OmpA transmembrane domain consisting of residues 1-171, by X-ray diffraction analysis, to a resolution of 2.5 A. It consists of a regular, extended eight-stranded beta-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. Surprisingly, the cavities seem to be highly conserved during evolution. The structure corroborates the concept that all outer membrane proteins consist of beta-barrels. The structure constitutes a beta-barrel membrane anchor that appears to be the outer membrane equivalent of the single-chain alpha-helix anchor of the inner membrane.


==Overview==
Structure of the outer membrane protein A transmembrane domain.,Pautsch A, Schulz GE Nat Struct Biol. 1998 Nov;5(11):1013-7. PMID:9808047<ref>PMID:9808047</ref>
The outer membrane protein A of Escherichia coli (OmpA) is an intensely studied example in the field of membrane protein folding. We have determined the structure of the OmpA transmembrane domain consisting of residues 1-171, by X-ray diffraction analysis, to a resolution of 2.5 A. It consists of a regular, extended eight-stranded beta-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. Surprisingly, the cavities seem to be highly conserved during evolution. The structure corroborates the concept that all outer membrane proteins consist of beta-barrels. The structure constitutes a beta-barrel membrane anchor that appears to be the outer membrane equivalent of the single-chain alpha-helix anchor of the inner membrane.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1BXW 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=1BXW OCA].
</div>
<div class="pdbe-citations 1bxw" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of the outer membrane protein A transmembrane domain., Pautsch A, Schulz GE, Nat Struct Biol. 1998 Nov;5(11):1013-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9808047 9808047]
*[[Porin 3D structures|Porin 3D structures]]
[[Category: Escherichia coli]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Pautsch, A.]]
__TOC__
[[Category: Schulz, G E.]]
</StructureSection>
[[Category: Outer membrane]]
[[Category: Large Structures]]
[[Category: Transmembrane protein]]
[[Category: Pautsch A]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:05:49 2008''
[[Category: Schulz GE]]
Retrieved from "https://proteopedia.org/1bxw"