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New page: left|200px<br /> <applet load="1oap" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oap, resolution 1.93Å" /> '''MAD STRUCTURE OF TH...
 
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[[Image:1oap.gif|left|200px]]<br />
<applet load="1oap" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1oap, resolution 1.93&Aring;" />
'''MAD STRUCTURE OF THE PERIPLASMIQUE DOMAIN OF THE ESCHERICHIA COLI PAL PROTEIN'''<br />


==About this Structure==
==Mad structure of the periplasmique domain of the Escherichia coli PAL protein==
1OAP is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OAP OCA]].  
<StructureSection load='1oap' size='340' side='right'caption='[[1oap]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oap]] 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=1OAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAP 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]] 1.93&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1oap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oap OCA], [https://pdbe.org/1oap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oap RCSB], [https://www.ebi.ac.uk/pdbsum/1oap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oap ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PAL_ECOLI PAL_ECOLI] Thought to play a role in bacterial envelope integrity. Very strongly associated with the peptidoglycan.
== 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/oa/1oap_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=1oap ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The peptidoglycan-associated lipoprotein (Pal) from Escherichia coli is part of the Tol--Pal multiprotein complex used by group A colicins to penetrate and kill cells. Pal homologues are found in many Gram-negative bacteria and the Tol--Pal system is thought to play a role in bacterial envelope integrity. The Pal protein comprises 152 amino acids. Crystals of the C-terminal 109-amino-acid fragment of the Pal protein have been produced. The crystals belong to the tetragonal space group I4(1), with unit-cell parameters a = b = 89.3, c = 67.2 A. There are two molecules in the asymmetric unit. Frozen crystals diffract to at least 2.8 A resolution using synchrotron radiation. Selenomethionine-substituted truncated Pal protein is currently being produced in order to use multiwavelength anomalous dispersion (MAD) for phasing.
 
Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli.,Abergel C, Walburger A, Chenivesse S, Lazdunski C Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):317-9. PMID:11173492<ref>PMID:11173492</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1oap" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Pal|Pal]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Abergel, C.]]
[[Category: Abergel C]]
[[Category: Bouveret, E.]]
[[Category: Bouveret E]]
[[Category: Claverie, J.M.]]
[[Category: Claverie JM]]
[[Category: Walburger, A.]]
[[Category: Walburger A]]
[[Category: SO4]]
[[Category: complete proteome]]
[[Category: lipoprotein]]
[[Category: outer membrane]]
[[Category: peptidoglycan binding]]
[[Category: periplasmic]]
[[Category: signal]]
[[Category: tol system]]
 
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Retrieved from "https://proteopedia.org/1oap"