8ag0

Crystal structure of mutant PRELID3a-TRIAP1 complex - R53E

spinqualitylabelsall models 8ag0, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ag0 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: BGC, GLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PLD3A_HUMAN Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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