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5xj6

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Current revision (10:18, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5xj6' size='340' side='right'caption='[[5xj6]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
<StructureSection load='5xj6' size='340' side='right'caption='[[5xj6]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xj6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJ6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XJ6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xj6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XJ6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G3P:SN-GLYCEROL-3-PHOSPHATE'>G3P</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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]] 2.37&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></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=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=G3P:SN-GLYCEROL-3-PHOSPHATE'>G3P</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xj5|5xj5]], [[5xj7|5xj7]], [[5xj8|5xj8]], [[5xj9|5xj9]]</td></tr>
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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=5xj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xj6 OCA], [https://pdbe.org/5xj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xj6 RCSB], [https://www.ebi.ac.uk/pdbsum/5xj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xj6 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xj6 OCA], [http://pdbe.org/5xj6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xj6 RCSB], [http://www.ebi.ac.uk/pdbsum/5xj6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xj6 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PLSY_AQUAE PLSY_AQUAE]] Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
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[https://www.uniprot.org/uniprot/PLSY_AQUAE PLSY_AQUAE] Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The membrane-integral glycerol 3-phosphate (G3P) acyltransferase PlsY catalyses the committed and essential step in bacterial phospholipid biosynthesis by acylation of G3P, forming lysophosphatidic acid. It contains no known acyltransferase motifs, lacks eukaryotic homologs, and uses the unusual acyl-phosphate as acyl donor, as opposed to acyl-CoA or acyl-carrier protein for other acyltransferases. Previous studies have identified several PlsY inhibitors as potential antimicrobials. Here we determine the crystal structure of PlsY at 1.48 A resolution, revealing a seven-transmembrane helix fold. Four additional substrate- and product-bound structures uncover the atomic details of its relatively inflexible active site. Structure and mutagenesis suggest a different acylation mechanism of 'substrate-assisted catalysis' that, unlike other acyltransferases, does not require a proteinaceous catalytic base to complete. The structure data and a high-throughput enzymatic assay developed in this work should prove useful for virtual and experimental screening of inhibitors against this vital bacterial enzyme.
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Structural insights into the committed step of bacterial phospholipid biosynthesis.,Li Z, Tang Y, Wu Y, Zhao S, Bao J, Luo Y, Li D Nat Commun. 2017 Nov 22;8(1):1691. doi: 10.1038/s41467-017-01821-9. PMID:29167463<ref>PMID:29167463</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 5xj6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aquifex aeolicus VF5]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Li, D]]
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[[Category: Li D]]
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[[Category: Li, Z]]
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[[Category: Li Z]]
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[[Category: Tang, Y]]
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[[Category: Tang Y]]
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[[Category: Glycerol 3-phosphate acyltransferase]]
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[[Category: Glycerylphosphate acyltransferase]]
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[[Category: Gpat]]
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[[Category: In meso]]
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[[Category: Lipid cubic phase]]
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[[Category: Lipid metabolism]]
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[[Category: Lipidic cubic phase]]
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[[Category: Monoacylglycerol]]
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[[Category: Phospholipid biosynthesis]]
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[[Category: Plsy]]
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[[Category: Substrate]]
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[[Category: Transferase]]
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[[Category: Ygih]]
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Current revision

Crystal structure of PlsY (YgiH), an integral membrane glycerol 3-phosphate acyltransferase - the glycerol 3-phosphate form

PDB ID 5xj6

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