8erp
From Proteopedia
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<table><tr><td colspan='2'>[[8erp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ERP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ERP FirstGlance]. <br> | <table><tr><td colspan='2'>[[8erp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ERP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ERP FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</td></tr> | ||
| - | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDC:[2-CYTIDYLATE-O-PHOSPHONYLOXYL]-ETHYL-TRIMETHYL-AMMONIUM'>CDC</scene>, <scene name='pdbligand=LBN: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDC:[2-CYTIDYLATE-O-PHOSPHONYLOXYL]-ETHYL-TRIMETHYL-AMMONIUM'>CDC</scene>, <scene name='pdbligand=LBN:(2R)-3-(hexadecanoyloxy)-2-{[(9Z)-octadec-9-enoyl]oxy}propyl+2-(trimethylazaniumyl)ethyl+phosphate'>LBN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8erp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8erp OCA], [https://pdbe.org/8erp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8erp RCSB], [https://www.ebi.ac.uk/pdbsum/8erp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8erp 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=8erp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8erp OCA], [https://pdbe.org/8erp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8erp RCSB], [https://www.ebi.ac.uk/pdbsum/8erp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8erp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/CHPT1_XENLA CHPT1_XENLA] Catalyzes phosphatidylcholine | + | [https://www.uniprot.org/uniprot/CHPT1_XENLA CHPT1_XENLA] Catalyzes the final step of de novo phosphatidylcholine (PC) synthesis, i.e. the transfer of choline phosphate from CDP-choline to the free hydroxyl of a diacylglycerol (DAG), producing a PC (PubMed:37179328). It thereby plays a central role in the formation and maintenance of vesicular membranes (By similarity). Shows a high preference for CDP-choline over CDP-ethanolamine as substrate (PubMed:37179328).[UniProtKB:Q8WUD6]<ref>PMID:37179328</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Phosphatidylcholine (PC) is the most abundant phospholipid in eukaryotic cell membranes. In eukaryotes, two highly homologous enzymes, cholinephosphotransferase-1 (CHPT1) and choline/ethanolamine phosphotransferase-1 (CEPT1) catalyze the final step of de novo PC synthesis. CHPT1/CEPT1 joins two substrates, cytidine diphosphate-choline (CDP-choline) and diacylglycerol (DAG), to produce PC, and Mg(2+) is required for the reaction. However, mechanisms of substrate recognition and catalysis remain unresolved. Here we report structures of a CHPT1 from Xenopus laevis (xlCHPT1) determined by cryo-electron microscopy to an overall resolution of ~3.2 A. xlCHPT1 forms a homodimer, and each protomer has 10 transmembrane helices (TMs). The first 6 TMs carve out a cone-shaped enclosure in the membrane in which the catalysis occurs. The enclosure opens to the cytosolic side, where a CDP-choline and two Mg(2+) are coordinated. The structures identify a catalytic site unique to eukaryotic CHPT1/CEPT1 and suggest an entryway for DAG. The structures also reveal an internal pseudo two-fold symmetry between TM3-6 and TM7-10, and suggest that CHPT1/CEPT1 may have evolved from their distant prokaryotic ancestors through gene duplication. | ||
| + | |||
| + | Structure of a eukaryotic cholinephosphotransferase-1 reveals mechanisms of substrate recognition and catalysis.,Wang L, Zhou M Nat Commun. 2023 May 13;14(1):2753. doi: 10.1038/s41467-023-38003-9. PMID:37179328<ref>PMID:37179328</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8erp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
| - | [[Category: | + | [[Category: Wang L]] |
| - | [[Category: | + | [[Category: Zhou M]] |
Current revision
Structure of Xenopus cholinephosphotransferase1 in complex with CDP-choline
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