8ctp

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'''Unreleased structure'''
 
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The entry 8ctp is ON HOLD until Paper Publication
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==Crystal structure of engineered phospholipase D mutant superPLD 2-23==
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<StructureSection load='8ctp' size='340' side='right'caption='[[8ctp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ctp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._PMF Streptomyces sp. PMF]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CTP FirstGlance]. <br>
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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]] 1.9&#8491;</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=PO4:PHOSPHATE+ION'>PO4</scene></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=8ctp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ctp OCA], [https://pdbe.org/8ctp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ctp RCSB], [https://www.ebi.ac.uk/pdbsum/8ctp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ctp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/P84147_STRSM P84147_STRSM]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cellular membranes contain numerous lipid species, and efforts to understand the biological functions of individual lipids have been stymied by a lack of approaches for controlled modulation of membrane composition in situ. Here we present a strategy for editing phospholipids, the most abundant lipids in biological membranes. Our membrane editor is based on a bacterial phospholipase D (PLD), which exchanges phospholipid head groups through hydrolysis or transphosphatidylation of phosphatidylcholine with water or exogenous alcohols. Exploiting activity-dependent directed enzyme evolution in mammalian cells, we have developed and structurally characterized a family of 'superPLDs' with up to a 100-fold enhancement in intracellular activity. We demonstrate the utility of superPLDs for both optogenetics-enabled editing of phospholipids within specific organelle membranes in live cells and biocatalytic synthesis of natural and unnatural designer phospholipids in vitro. Beyond the superPLDs, activity-based directed enzyme evolution in mammalian cells is a generalizable approach to engineer additional chemoenzymatic biomolecule editors.
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Authors:
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Activity-based directed evolution of a membrane editor in mammalian cells.,Tei R, Bagde SR, Fromme JC, Baskin JM Nat Chem. 2023 Jul;15(7):1030-1039. doi: 10.1038/s41557-023-01214-0. Epub 2023 , May 22. PMID:37217787<ref>PMID:37217787</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8ctp" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Phospholipase D 3D structures|Phospholipase D 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptomyces sp. PMF]]
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[[Category: Bagde SR]]
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[[Category: Baskin JM]]
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[[Category: Fromme JC]]
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[[Category: Tei R]]

Current revision

Crystal structure of engineered phospholipase D mutant superPLD 2-23

PDB ID 8ctp

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