6E0H
PDB: afTMEM16 reconstituted in nanodiscs in the presence of Ca2+
6E0H の概要
| エントリーDOI | 10.2210/pdb6e0h/pdb |
| 関連するPDBエントリー | 6E1O |
| EMDBエントリー | 8948 8959 |
| 分子名称 | Plasma membrane channel protein (Aqy1), putative, CALCIUM ION (2 entities in total) |
| 機能のキーワード | scramblase, ca2+-activated, membrane-reorganization, lipid transport |
| 由来する生物種 | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 169394.03 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (4.05 Å) |
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