8VC2
CryoEM structure of insect gustatory receptor BmGr9 in the presence of fructose
8VC2 の概要
| エントリーDOI | 10.2210/pdb8vc2/pdb |
| EMDBエントリー | 43130 |
| 分子名称 | Gustatory receptor, (7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-17,20-DIEN-1-AMINIUM 4-OXIDE (2 entities in total) |
| 機能のキーワード | gustatory receptor, homotetramer, ligand-gated ion channel, seven transmembrane, membrane protein |
| 由来する生物種 | Bombyx mori (domestic silkworm) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 221325.55 |
| 構造登録者 | Frank, H.M.,Walsh Jr., R.M.,Garrity, P.A.,Gaudet, R. (登録日: 2023-12-13, 公開日: 2024-01-10, 最終更新日: 2024-12-18) |
| 主引用文献 | Frank, H.M.,Walujkar, S.,Walsh Jr., R.M.,Laursen, W.J.,Theobald, D.L.,Garrity, P.A.,Gaudet, R. Structural basis of ligand specificity and channel activation in an insect gustatory receptor. Cell Rep, 43:114035-114035, 2024 Cited by PubMed Abstract: Gustatory receptors (GRs) are critical for insect chemosensation and are potential targets for controlling pests and disease vectors, making their structural investigation a vital step toward such applications. We present structures of Bombyx mori Gr9 (BmGr9), a fructose-gated cation channel, in agonist-free and fructose-bound states. BmGr9 forms a tetramer similar to distantly related insect odorant receptors (ORs). Upon fructose binding, BmGr9's channel gate opens through helix S7b movements. In contrast to ORs, BmGr9's ligand-binding pocket, shaped by a kinked helix S4 and a shorter extracellular S3-S4 loop, is larger and solvent accessible in both agonist-free and fructose-bound states. Also, unlike ORs, fructose binding by BmGr9 involves helix S5 and a pocket lined with aromatic and polar residues. Structure-based sequence alignments reveal distinct patterns of ligand-binding pocket residue conservation in GR subfamilies associated with different ligand classes. These data provide insight into the molecular basis of GR ligand specificity and function. PubMed: 38573859DOI: 10.1016/j.celrep.2024.114035 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.98 Å) |
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