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| | ==Crystal Structure of the 1-acyl-sn-glycerophosphate (LPA) acyltransferase, PlsC, from Thermotoga maritima== | | ==Crystal Structure of the 1-acyl-sn-glycerophosphate (LPA) acyltransferase, PlsC, from Thermotoga maritima== |
| - | <StructureSection load='5kym' size='340' side='right' caption='[[5kym]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='5kym' size='340' side='right'caption='[[5kym]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5kym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KYM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5kym]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KYM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DD9:NONANE'>DD9</scene>, <scene name='pdbligand=HGX:1-HEPTADECANOYL-2-TRIDECANOYL-3-GLYCEROL-PHOSPHONYL+CHOLINE'>HGX</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</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]] 2.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tmari_1701 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DD9:NONANE'>DD9</scene>, <scene name='pdbligand=HGX:1-HEPTADECANOYL-2-TRIDECANOYL-3-GLYCEROL-PHOSPHONYL+CHOLINE'>HGX</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1-acylglycerol-3-phosphate_O-acyltransferase 1-acylglycerol-3-phosphate O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.51 2.3.1.51] </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=5kym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kym OCA], [https://pdbe.org/5kym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kym RCSB], [https://www.ebi.ac.uk/pdbsum/5kym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kym 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=5kym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kym OCA], [http://pdbe.org/5kym PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kym RCSB], [http://www.ebi.ac.uk/pdbsum/5kym PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kym ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9X219_THEMA Q9X219_THEMA] |
| | <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: 1-acylglycerol-3-phosphate O-acyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Thema]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Gajewski, S]] | + | [[Category: Gajewski S]] |
| - | [[Category: Kumar, G]] | + | [[Category: Kumar G]] |
| - | [[Category: Martin, E W]] | + | [[Category: Martin EW]] |
| - | [[Category: Robertson, R M]] | + | [[Category: Robertson RM]] |
| - | [[Category: Rock, C O]] | + | [[Category: Rock CO]] |
| - | [[Category: White, S W]] | + | [[Category: White SW]] |
| - | [[Category: Yao, J]] | + | [[Category: Yao J]] |
| - | [[Category: 1-acyl-sn-glycerol-3-phosphate acyltransferase]]
| + | |
| - | [[Category: Alpha-beta structure]]
| + | |
| - | [[Category: Hx4d acyltransferase]]
| + | |
| - | [[Category: Integral membrane]]
| + | |
| - | [[Category: Membrane helice]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q9X219_THEMA
Publication Abstract from PubMed
Phosphatidic acid (PA), the central intermediate in membrane phospholipid synthesis, is generated by two acyltransferases in a pathway conserved in all life forms. The second step in this pathway is catalyzed by 1-acyl-sn-glycerol-3-phosphate acyltransferase, called PlsC in bacteria. Here we present the crystal structure of PlsC from Thermotoga maritima, revealing an unusual hydrophobic/aromatic N-terminal two-helix motif linked to an acyltransferase alphabeta-domain that contains the catalytic HX4D motif. PlsC dictates the acyl chain composition of the 2-position of phospholipids, and the acyl chain selectivity 'ruler' is an appropriately placed and closed hydrophobic tunnel. We confirmed this by site-directed mutagenesis and membrane composition analysis of Escherichia coli cells that expressed mutant PlsC. Molecular dynamics (MD) simulations showed that the two-helix motif represents a novel substructure that firmly anchors the protein to one leaflet of the membrane. This binding mode allows the PlsC active site to acylate lysophospholipids within the membrane bilayer by using soluble acyl donors.
A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer.,Robertson RM, Yao J, Gajewski S, Kumar G, Martin EW, Rock CO, White SW Nat Struct Mol Biol. 2017 Jul 17. doi: 10.1038/nsmb.3436. PMID:28714993[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Robertson RM, Yao J, Gajewski S, Kumar G, Martin EW, Rock CO, White SW. A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer. Nat Struct Mol Biol. 2017 Jul 17. doi: 10.1038/nsmb.3436. PMID:28714993 doi:http://dx.doi.org/10.1038/nsmb.3436
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