1oap
From Proteopedia
(Difference between revisions)
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<StructureSection load='1oap' size='340' side='right'caption='[[1oap]], [[Resolution|resolution]] 1.93Å' scene=''> | <StructureSection load='1oap' size='340' side='right'caption='[[1oap]], [[Resolution|resolution]] 1.93Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1oap]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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="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. | ||
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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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1oap" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Pal|Pal]] | *[[Pal|Pal]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Abergel | + | [[Category: Abergel C]] |
| - | [[Category: Bouveret | + | [[Category: Bouveret E]] |
| - | [[Category: Claverie | + | [[Category: Claverie JM]] |
| - | [[Category: Walburger | + | [[Category: Walburger A]] |
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Revision as of 08:56, 10 April 2024
Mad structure of the periplasmique domain of the Escherichia coli PAL protein
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