6E0H
PDB: afTMEM16 reconstituted in nanodiscs in the presence of Ca2+
Summary for 6E0H
| Entry DOI | 10.2210/pdb6e0h/pdb |
| Related | 6E1O |
| EMDB information | 8948 8959 |
| Descriptor | Plasma membrane channel protein (Aqy1), putative, CALCIUM ION (2 entities in total) |
| Functional Keywords | scramblase, ca2+-activated, membrane-reorganization, lipid transport |
| Biological source | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Total number of polymer chains | 2 |
| Total formula weight | 169394.03 |
| Authors | Falzone, M.E.,Accardi, A. (deposition date: 2018-07-06, release date: 2019-02-06, Last modification date: 2024-03-13) |
| Primary citation | Falzone, M.E.,Rheinberger, J.,Lee, B.C.,Peyear, T.,Sasset, L.,Raczkowski, A.M.,Eng, E.T.,Di Lorenzo, A.,Andersen, O.S.,Nimigean, C.M.,Accardi, A. Structural basis of Ca2+-dependent activation and lipid transport by a TMEM16 scramblase. Elife, 8:-, 2019 Cited by PubMed Abstract: The lipid distribution of plasma membranes of eukaryotic cells is asymmetric and phospholipid scramblases disrupt this asymmetry by mediating the rapid, nonselective transport of lipids down their concentration gradients. As a result, phosphatidylserine is exposed to the outer leaflet of membrane, an important step in extracellular signaling networks controlling processes such as apoptosis, blood coagulation, membrane fusion and repair. Several TMEM16 family members have been identified as Ca-activated scramblases, but the mechanisms underlying their Ca-dependent gating and their effects on the surrounding lipid bilayer remain poorly understood. Here, we describe three high-resolution cryo-electron microscopy structures of a fungal scramblase from , afTMEM16, reconstituted in lipid nanodiscs. These structures reveal that Ca-dependent activation of the scramblase entails global rearrangement of the transmembrane and cytosolic domains. These structures, together with functional experiments, suggest that activation of the protein thins the membrane near the transport pathway to facilitate rapid transbilayer lipid movement. PubMed: 30648972DOI: 10.7554/eLife.43229 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.05 Å) |
Structure validation
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