8ag0

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m (Protected "8ag0" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 8ag0 is ON HOLD
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==Crystal structure of mutant PRELID3a-TRIAP1 complex - R53E==
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<StructureSection load='8ag0' size='340' side='right'caption='[[8ag0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ag0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AG0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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=8ag0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ag0 OCA], [https://pdbe.org/8ag0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ag0 RCSB], [https://www.ebi.ac.uk/pdbsum/8ag0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ag0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PLD3A_HUMAN PLD3A_HUMAN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The PRELID-TRIAP1 family of proteins is responsible for lipid transfer in mitochondria. Multiple structures have been resolved of apo and lipid substrate bound forms, allowing us to begin to piece together the molecular level details of the full lipid transfer cycle. Here, we used molecular dynamics simulations to demonstrate that the lipid binding is mediated by an extended, water-mediated hydrogen bonding network. A key mutation, R53E, was found to disrupt this network, causing lipid to be released from the complex. The X-ray crystal structure of R53E was captured in a fully closed and apo state. Lipid transfer assays and molecular simulations allow us to interpret the observed conformation in the context of the biological role. Together, our work provides further understanding of the mechanistic control of lipid transport by PRELID-TRIAP1 in mitochondria.
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Authors: Milara, X., Perez-Dorado, J.I., Matthews, S.J.
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An intermolecular hydrogen bonded network in the PRELID-TRIAP protein family plays a role in lipid sensing.,Miliara X, Tatsuta T, Eiyama A, Langer T, Rouse SL, Matthews S Biochim Biophys Acta Proteins Proteom. 2023 Jan 1;1871(1):140867. doi: , 10.1016/j.bbapap.2022.140867. Epub 2022 Oct 26. PMID:36309326<ref>PMID:36309326</ref>
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Description: Crystal structure of mutant PRELID3a-TRIAP1 complex -R53E
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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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[[Category: Matthews, S.J]]
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<div class="pdbe-citations 8ag0" style="background-color:#fffaf0;"></div>
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[[Category: Milara, X]]
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== References ==
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[[Category: Perez-Dorado, J.I]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Matthews SJ]]
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[[Category: Milara X]]
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[[Category: Perez-Dorado JI]]

Revision as of 10:13, 24 November 2022

Crystal structure of mutant PRELID3a-TRIAP1 complex - R53E

PDB ID 8ag0

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