1u7n
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:1u7n.png|left|200px]] | ||
| - | < | + | ==Crystal Structure of the fatty acid/phospholipid synthesis protein PlsX from Enterococcus faecalis V583== |
| - | + | <StructureSection load='1u7n' size='340' side='right'caption='[[1u7n]], [[Resolution|resolution]] 2.26Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[1u7n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U7N FirstGlance]. <br> | |
| - | or | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26Å</td></tr> |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1u7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u7n OCA], [https://pdbe.org/1u7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u7n RCSB], [https://www.ebi.ac.uk/pdbsum/1u7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u7n ProSAT], [https://www.topsan.org/Proteins/MCSG/1u7n TOPSAN]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PLSX_ENTFA PLSX_ENTFA] Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA (By similarity).[HAMAP-Rule:MF_00019] | ||
| + | == 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/u7/1u7n_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1u7n ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | PlsX is a key enzyme that coordinates the production of fatty acids and membrane phospholipids. The plsX gene is co-localized with a bacterial fab gene cluster which encodes several key fatty acid biosynthetic enzymes. The protein is a member of a large, conserved protein family (Pfam02504) found exclusively in bacteria. The PlsX sequence homologues include both phosphate acetyltransferases and phosphate butaryltransferases that catalyze the transfer of an acetyl or butaryl group to orthophosphate. We have determined the crystal structure of PlsX from the human pathogen Enterococcus faecalis. PlsX is a alpha/beta/alpha sandwich that resembles a Rossmann fold and forms a dimer. A putative catalytic site has been identified within a deep groove on the interface between monomers. This site showed strong surface similarity to epimerases and reductases. It was recently proposed that PlsX is a phosphate acyltransferase that catalyzes the formation of acyl-phosphate from the acyl-acyl carrier protein; however the specific biochemical function of the PlsX protein awaits further experimental scrutiny. | ||
| - | + | Crystal structure of fatty acid/phospholipid synthesis protein PlsX from Enterococcus faecalis.,Kim Y, Li H, Binkowski TA, Holzle D, Joachimiak A J Struct Funct Genomics. 2009 Apr;10(2):157-63. Epub 2008 Dec 5. PMID:19058030<ref>PMID:19058030</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1u7n" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
| - | [[Category: Collart | + | [[Category: Large Structures]] |
| - | [[Category: Joachimiak | + | [[Category: Collart F]] |
| - | [[Category: Kim | + | [[Category: Joachimiak A]] |
| - | [[Category: Li | + | [[Category: Kim Y]] |
| - | + | [[Category: Li H]] | |
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Current revision
Crystal Structure of the fatty acid/phospholipid synthesis protein PlsX from Enterococcus faecalis V583
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