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4q2e

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==CRYSTAL STRUCTURE OF AN INTRAMEMBRANE CDP-DAG SYNTHETASE CENTRAL FOR PHOSPHOLIPID BIOSYNTHESIS (S200C/S258C, active mutant)==
==CRYSTAL STRUCTURE OF AN INTRAMEMBRANE CDP-DAG SYNTHETASE CENTRAL FOR PHOSPHOLIPID BIOSYNTHESIS (S200C/S258C, active mutant)==
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<StructureSection load='4q2e' size='340' side='right' caption='[[4q2e]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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<StructureSection load='4q2e' size='340' side='right'caption='[[4q2e]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4q2e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q2E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4q2e]] 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=4Q2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q2E FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 3.4&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidate_cytidylyltransferase Phosphatidate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.41 2.7.7.41] </span></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=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<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=4q2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q2e RCSB], [http://www.ebi.ac.uk/pdbsum/4q2e PDBsum]</span></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=4q2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2e OCA], [https://pdbe.org/4q2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q2e RCSB], [https://www.ebi.ac.uk/pdbsum/4q2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q2e ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CDSA_THEMA CDSA_THEMA]
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Phospholipids are elemental building-block molecules for biological membranes. Biosynthesis of phosphatidylinositol, phosphatidylglycerol and phosphatidylserine requires a central liponucleotide intermediate named cytidine-diphosphate diacylglycerol (CDP-DAG). The CDP-DAG synthetase (Cds) is an integral membrane enzyme catalysing the formation of CDP-DAG, an essential step for phosphoinositide recycling during signal transduction. Here we report the structure of the Cds from Thermotoga maritima (TmCdsA) at 3.4 A resolution. TmCdsA forms a homodimer and each monomer contains nine transmembrane helices arranged into a novel fold with three domains. An unusual funnel-shaped cavity penetrates half way into the membrane, allowing the enzyme to simultaneously accept hydrophilic substrate (cytidine 5'-triphosphate (CTP)/deoxy-CTP) from cytoplasm and hydrophobic substrate (phosphatidic acid) from membrane. Located at the bottom of the cavity, a Mg(2+)-K(+) hetero-di-metal centre coordinated by an Asp-Asp dyad serves as the cofactor of TmCdsA. The results suggest a two-metal-ion catalytic mechanism for the Cds-mediated synthesis of CDP-DAG at the membrane-cytoplasm interface.
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Structure and mechanism of an intramembrane liponucleotide synthetase central for phospholipid biosynthesis.,Liu X, Yin Y, Wu J, Liu Z Nat Commun. 2014 Jun 27;5:4244. doi: 10.1038/ncomms5244. PMID:24968740<ref>PMID:24968740</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Phosphatidate cytidylyltransferase]]
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[[Category: Large Structures]]
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[[Category: Liu, X]]
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[[Category: Thermotoga maritima MSB8]]
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[[Category: Liu, Z]]
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[[Category: Liu X]]
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[[Category: Wu, J]]
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[[Category: Liu Z]]
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[[Category: Yin, Y]]
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[[Category: Wu J]]
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[[Category: Cdsa fold]]
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[[Category: Yin Y]]
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[[Category: Ctp and phosphatidic acid binding]]
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[[Category: Intramembrane enzyme]]
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[[Category: Membrane]]
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[[Category: Nucleotidyltransferase]]
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[[Category: Phospholipid biosynthesis lipid metabolism]]
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[[Category: Transferase]]
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Current revision

CRYSTAL STRUCTURE OF AN INTRAMEMBRANE CDP-DAG SYNTHETASE CENTRAL FOR PHOSPHOLIPID BIOSYNTHESIS (S200C/S258C, active mutant)

PDB ID 4q2e

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