1oap

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[[Image:1oap.gif|left|200px]]
 
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==Mad structure of the periplasmique domain of the Escherichia coli PAL protein==
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The line below this paragraph, containing "STRUCTURE_1oap", creates the "Structure Box" on the page.
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<StructureSection load='1oap' size='340' side='right'caption='[[1oap]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_1oap| PDB=1oap | SCENE= }}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PAL_ECOLI PAL_ECOLI] Thought to play a role in bacterial envelope integrity. Very strongly associated with the peptidoglycan.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oap_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''MAD STRUCTURE OF THE PERIPLASMIQUE DOMAIN OF THE ESCHERICHIA COLI PAL PROTEIN'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1oap" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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1OAP 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=1OAP OCA].
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*[[Pal|Pal]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Abergel, C.]]
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[[Category: Abergel C]]
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[[Category: Bouveret, E.]]
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[[Category: Bouveret E]]
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[[Category: Claverie, J M.]]
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[[Category: Claverie JM]]
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[[Category: Walburger, A.]]
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[[Category: Walburger A]]
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[[Category: Complete proteome]]
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[[Category: Lipoprotein]]
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[[Category: Outer membrane]]
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[[Category: Peptidoglycan binding]]
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[[Category: Periplasmic]]
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[[Category: Signal]]
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[[Category: Tol system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:36:12 2008''
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Current revision

Mad structure of the periplasmique domain of the Escherichia coli PAL protein

PDB ID 1oap

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