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| | ==Crystal structure of PlsY (YgiH), an integral membrane glycerol 3-phosphate acyltransferase - the lysphosphatidic acid form== | | ==Crystal structure of PlsY (YgiH), an integral membrane glycerol 3-phosphate acyltransferase - the lysphosphatidic acid form== |
| - | <StructureSection load='5xj8' size='340' side='right' caption='[[5xj8]], [[Resolution|resolution]] 2.41Å' scene=''> | + | <StructureSection load='5xj8' size='340' side='right'caption='[[5xj8]], [[Resolution|resolution]] 2.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xj8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XJ8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xj8]] is a 2 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=5XJ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XJ8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NKO:(2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL+HEXADECANOATE'>NKO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.41Å</td></tr> |
| - | <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> | + | <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=NKO:(2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL+HEXADECANOATE'>NKO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xj5|5xj5]], [[5xj6|5xj6]], [[5xj7|5xj7]], [[5xj9|5xj9]]</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=5xj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xj8 OCA], [https://pdbe.org/5xj8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xj8 RCSB], [https://www.ebi.ac.uk/pdbsum/5xj8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xj8 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xj8 OCA], [http://pdbe.org/5xj8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xj8 RCSB], [http://www.ebi.ac.uk/pdbsum/5xj8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xj8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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. | + | [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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Li, D]] | + | [[Category: Aquifex aeolicus VF5]] |
| - | [[Category: Li, Z]] | + | [[Category: Large Structures]] |
| - | [[Category: Tang, Y]] | + | [[Category: Li D]] |
| - | [[Category: 1-hexadecanoyl-sn-glycero-3-phosphate]] | + | [[Category: Li Z]] |
| - | [[Category: 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphate]] | + | [[Category: Tang Y]] |
| - | [[Category: 16:0 lyso pa]]
| + | |
| - | [[Category: Glycerylphosphate acyltransferase]]
| + | |
| - | [[Category: Gpat]]
| + | |
| - | [[Category: In meso]]
| + | |
| - | [[Category: Lipid cubic phase]]
| + | |
| - | [[Category: Lipid metabolism]]
| + | |
| - | [[Category: Lipidic cubic phase]]
| + | |
| - | [[Category: Lpa]]
| + | |
| - | [[Category: Lyso pa]]
| + | |
| - | [[Category: Lysopa]]
| + | |
| - | [[Category: Lysophophatidic acid]]
| + | |
| - | [[Category: Monoacylglycerol]]
| + | |
| - | [[Category: Palmitoyl lysophosphatidic acid]]
| + | |
| - | [[Category: Phospholipid biosynthesis]]
| + | |
| - | [[Category: Plsy]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Ygih]]
| + | |
| Structural highlights
Function
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.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li Z, Tang Y, Wu Y, Zhao S, Bao J, Luo Y, Li D. Structural insights into the committed step of bacterial phospholipid biosynthesis. Nat Commun. 2017 Nov 22;8(1):1691. doi: 10.1038/s41467-017-01821-9. PMID:29167463 doi:http://dx.doi.org/10.1038/s41467-017-01821-9
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