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[[Image:1qjp.jpg|left|200px]]
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{{STRUCTURE_1qjp|  PDB=1qjp  |  SCENE=  }}
'''HIGH RESOLUTION STRUCTURE OF THE OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN'''


==HIGH RESOLUTION STRUCTURE OF THE OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN==
<StructureSection load='1qjp' size='340' side='right'caption='[[1qjp]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qjp]] 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=1QJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QJP 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]] 1.65&#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=1qjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjp OCA], [https://pdbe.org/1qjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qjp RCSB], [https://www.ebi.ac.uk/pdbsum/1qjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qjp 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/qj/1qjp_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=1qjp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The membrane domain of OmpA consists of an eight-stranded all-next-neighbor antiparallel beta-barrel with short turns at the periplasmic barrel end and long flexible loops at the external end. The structure analysis has been extended from medium resolution to 1. 65 A (1 A=0.1 nm), and the molecular model has been refined anisotropically to show oriented mobilities of the structural elements. The improved data allowed us to locate five further detergent molecules and 11 more water molecules. Moreover, the two large non-polar packing contacts have now been defined in detail. The analysis indicates that the beta-barrel constitutes a solid scaffold such that the long external loops need not contribute to stability. These loops are highly mobile and thus cause a major problem during the crystallization process. The beta-barrel was related to those of lipocalins. Two further crystal forms with exceptionally dense packing arrangements were established at medium resolution.


==Overview==
High-resolution structure of the OmpA membrane domain.,Pautsch A, Schulz GE J Mol Biol. 2000 Apr 28;298(2):273-82. PMID:10764596<ref>PMID:10764596</ref>
The membrane domain of OmpA consists of an eight-stranded all-next-neighbor antiparallel beta-barrel with short turns at the periplasmic barrel end and long flexible loops at the external end. The structure analysis has been extended from medium resolution to 1. 65 A (1 A=0.1 nm), and the molecular model has been refined anisotropically to show oriented mobilities of the structural elements. The improved data allowed us to locate five further detergent molecules and 11 more water molecules. Moreover, the two large non-polar packing contacts have now been defined in detail. The analysis indicates that the beta-barrel constitutes a solid scaffold such that the long external loops need not contribute to stability. These loops are highly mobile and thus cause a major problem during the crystallization process. The beta-barrel was related to those of lipocalins. Two further crystal forms with exceptionally dense packing arrangements were established at medium resolution.


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


==Reference==
==See Also==
High-resolution structure of the OmpA membrane domain., Pautsch A, Schulz GE, J Mol Biol. 2000 Apr 28;298(2):273-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10764596 10764596]
*[[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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:21:22 2008''
[[Category: Pautsch A]]
[[Category: Schulz GE]]
Retrieved from "https://proteopedia.org/1qjp"