5T4X
CRYSTAL STRUCTURE OF PDE6D IN APO-STATE
5T4X の概要
| エントリーDOI | 10.2210/pdb5t4x/pdb |
| 分子名称 | Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta (2 entities in total) |
| 機能のキーワード | immunoglobulin-like beta sandwitch, pde6 delta, farnesyl, lipid binding protein, prenyl binding protein, geranylgeranyl, transport protein, phosphodiesterase 6, rhodopsin, membrane dissociation, apo-state, membrane trafficking, cellular trafficking, rhodopsin kinase, ras-gtpase |
| 由来する生物種 | Mus musculus (Mouse) |
| 細胞内の位置 | Cytoplasm, cytosol : O55057 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 19540.31 |
| 構造登録者 | |
| 主引用文献 | Qureshi, B.M.,Schmidt, A.,Behrmann, E.,Burger, J.,Mielke, T.,Spahn, C.M.T.,Heck, M.,Scheerer, P. Mechanistic insights into the role of prenyl-binding protein PrBP/ delta in membrane dissociation of phosphodiesterase 6. Nat Commun, 9:90-90, 2018 Cited by PubMed Abstract: Isoprenylated proteins are associated with membranes and their inter-compartmental distribution is regulated by solubilization factors, which incorporate lipid moieties in hydrophobic cavities and thereby facilitate free diffusion during trafficking. Here we report the crystal structure of a solubilization factor, the prenyl-binding protein (PrBP/δ), at 1.81 Å resolution in its ligand-free apo-form. Apo-PrBP/δ harbors a preshaped, deep hydrophobic cavity, capacitating apo-PrBP/δ to readily bind its prenylated cargo. To investigate the molecular mechanism of cargo solubilization we analyzed the PrBP/δ-induced membrane dissociation of rod photoreceptor phosphodiesterase (PDE6). The results suggest that PrBP/δ exclusively interacts with the soluble fraction of PDE6. Depletion of soluble species in turn leads to dissociation of membrane-bound PDE6, as both are in equilibrium. This "solubilization by depletion" mechanism of PrBP/δ differs from the extraction of prenylated proteins by the similar folded solubilization factor RhoGDI, which interacts with membrane bound cargo via an N-terminal structural element lacking in PrBP/δ. PubMed: 29311697DOI: 10.1038/s41467-017-02569-y 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.81 Å) |
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