6I9K
Crystal structure of Jumping Spider Rhodopsin-1 bound to 9-cis retinal
6I9K の概要
| エントリーDOI | 10.2210/pdb6i9k/pdb |
| 分子名称 | Kumopsin1, RETINAL, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (4 entities in total) |
| 機能のキーワード | rhodopsin, gpcr, light-sensitive, retinal, membrane protein |
| 由来する生物種 | Hasarius adansoni |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 46802.67 |
| 構造登録者 | Varma, N.,Mutt, E.,Muehle, J.,Panneels, V.,Terakita, A.,Deupi, X.,Nogly, P.,Schertler, F.X.G.,Lesca, E. (登録日: 2018-11-23, 公開日: 2019-07-03, 最終更新日: 2024-10-23) |
| 主引用文献 | Varma, N.,Mutt, E.,Muhle, J.,Panneels, V.,Terakita, A.,Deupi, X.,Nogly, P.,Schertler, G.F.X.,Lesca, E. Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR. Proc.Natl.Acad.Sci.USA, 116:14547-14556, 2019 Cited by PubMed Abstract: Light-sensitive G protein-coupled receptors (GPCRs)-rhodopsins-absorb photons to isomerize their covalently bound retinal, triggering conformational changes that result in downstream signaling cascades. Monostable rhodopsins release retinal upon isomerization as opposed to the retinal in bistable rhodopsins that "reisomerize" upon absorption of a second photon. Understanding the mechanistic differences between these light-sensitive GPCRs has been hindered by the scarcity of recombinant models of the latter. Here, we reveal the high-resolution crystal structure of a recombinant bistable rhodopsin, jumping spider rhodopsin-1, bound to the inverse agonist 9- retinal. We observe a water-mediated network around the ligand hinting toward the basis of their bistable nature. In contrast to bovine rhodopsin (monostable), the transmembrane bundle of jumping spider rhodopsin-1 as well that of the bistable squid rhodopsin adopts a more "activation-ready" conformation often observed in other nonphotosensitive class A GPCRs. These similarities suggest the role of jumping spider rhodopsin-1 as a potential model system in the study of the structure-function relationship of both photosensitive and nonphotosensitive class A GPCRs. PubMed: 31249143DOI: 10.1073/pnas.1902192116 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.145 Å) |
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