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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography	An intermolecular hydrogen bonded network in the PRELID-TRIAP protein family plays a role in lipid sensing Xeni Miliara , Takashi Tatsuta , Akinori Eiyama , Thomas Langer , Sarah L. Rouse , Steve Matthews Biochimica Et Biophysica Acta (bba) - Proteins And Proteomics 1871 DOI: 10.1016/j.bbapap.2022.140867 Diamond Proposal Number(s): [9424] Open Access Show Abstract ▼ Abstract: 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.	Nov 2022
I03-Macromolecular Crystallography I04-Macromolecular Crystallography	Structural comparison of yeast and human intra-mitochondrial lipid transport systems Xeni Miliara , Stephen Matthews Biochemical Society Transactions 44, 479 - 485 DOI: 10.1042/BST20150264 Diamond Proposal Number(s): [9424, 12579] Open Access Show Abstract ▼ Abstract: Mitochondria depend on a tightly regulated supply of phospholipids. The protein of relevant evolutionary and lymphoid interest (PRELI)/Ups1 family together with its mitochondrial chaperones [TP53-regulated inhibitor of apoptosis 1 (TRIAP1)/Mdm35] represents a unique heterodimeric lipid-transfer system that is evolutionary conserved from yeast to man. Recent X-ray crystal structures of the human and yeast systems are compared and discuss here and shed new insight into the mechanism of the PRELI/Ups1 system.	Apr 2016

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