6f8e

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m (Protected "6f8e" [edit=sysop:move=sysop])
Current revision (06:04, 19 June 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6f8e is ON HOLD
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==PH domain from TgAPH==
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<StructureSection load='6f8e' size='340' side='right'caption='[[6f8e]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6f8e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii_ME49 Toxoplasma gondii ME49]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F8E 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">Solution NMR</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=6f8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f8e OCA], [https://pdbe.org/6f8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f8e RCSB], [https://www.ebi.ac.uk/pdbsum/6f8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f8e ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A125YY72_TOXGM A0A125YY72_TOXGM]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Plasmodium falciparum and Toxoplasma gondii are obligate intracellular parasites that belong to the phylum of Apicomplexa and cause major human diseases. Their access to an intracellular lifestyle is reliant on the coordinated release of proteins from the specialized apical organelles called micronemes and rhoptries. A specific phosphatidic acid effector, the acylated pleckstrin homology domain-containing protein (APH) plays a central role in microneme exocytosis and thus is essential for motility, cell entry, and egress. TgAPH is acylated on the surface of the micronemes and recruited to phosphatidic acid (PA)-enriched membranes. Here, we dissect the atomic details of APH PA-sensing hub and its functional interaction with phospholipid membranes. We unravel the key determinant of PA recognition for the first time and show that APH inserts into and clusters multiple phosphate head-groups at the bilayer binding surface.
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Authors:
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Structural Basis of Phosphatidic Acid Sensing by APH in Apicomplexan Parasites.,Darvill N, Dubois DJ, Rouse SL, Hammoudi PM, Blake T, Benjamin S, Liu B, Soldati-Favre D, Matthews S Structure. 2018 Aug 7;26(8):1059-1071.e6. doi: 10.1016/j.str.2018.05.001. Epub, 2018 Jun 14. PMID:29910186<ref>PMID:29910186</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 6f8e" style="background-color:#fffaf0;"></div>
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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: Toxoplasma gondii ME49]]
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[[Category: Benjamin S]]
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[[Category: Blake T]]
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[[Category: Darvill N]]
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[[Category: Dubois DJ]]
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[[Category: Hammoudi PM]]
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[[Category: Liu B]]
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[[Category: Matthews S]]
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[[Category: Pino P]]
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[[Category: Rouse S]]
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[[Category: Soldati-Favre D]]

Current revision

PH domain from TgAPH

PDB ID 6f8e

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