8AG8
Structure of the Fluorescence Recovery-like protein FRPL from Pseudomonas borbori
8AG8 の概要
| エントリーDOI | 10.2210/pdb8ag8/pdb |
| 分子名称 | Fluorescence Recovery-like protein, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID (3 entities in total) |
| 機能のキーワード | stress-related, alpha-helical bundle, dimer, protein binding |
| 由来する生物種 | Pseudomonas borbori |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 13610.59 |
| 構造登録者 | |
| 主引用文献 | Steube, N.,Moldenhauer, M.,Weiland, P.,Saman, D.,Kilb, A.,Ramirez Rojas, A.A.,Garg, S.G.,Schindler, D.,Graumann, P.L.,Benesch, J.L.P.,Bange, G.,Friedrich, T.,Hochberg, G.K.A. Fortuitously compatible protein surfaces primed allosteric control in cyanobacterial photoprotection. Nat Ecol Evol, 7:756-767, 2023 Cited by PubMed Abstract: Highly specific interactions between proteins are a fundamental prerequisite for life, but how they evolve remains an unsolved problem. In particular, interactions between initially unrelated proteins require that they evolve matching surfaces. It is unclear whether such surface compatibilities can only be built by selection in small incremental steps, or whether they can also emerge fortuitously. Here, we used molecular phylogenetics, ancestral sequence reconstruction and biophysical characterization of resurrected proteins to retrace the evolution of an allosteric interaction between two proteins that act in the cyanobacterial photoprotection system. We show that this interaction between the orange carotenoid protein (OCP) and its unrelated regulator, the fluorescence recovery protein (FRP), evolved when a precursor of FRP was horizontally acquired by cyanobacteria. FRP's precursors could already interact with and regulate OCP even before these proteins first encountered each other in an ancestral cyanobacterium. The OCP-FRP interaction exploits an ancient dimer interface in OCP, which also predates the recruitment of FRP into the photoprotection system. Together, our work shows how evolution can fashion complex regulatory systems easily out of pre-existing components. PubMed: 37012377DOI: 10.1038/s41559-023-02018-8 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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