6f8e | pdb_00006f8e

PH domain from TgAPH

spinqualitylabelsall models 6f8e, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6f8e is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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