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8AG8

Structure of the Fluorescence Recovery-like protein FRPL from Pseudomonas borbori

8AG8 の概要
エントリーDOI10.2210/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
Weiland, P.,Bange, G. (登録日: 2022-07-19, 公開日: 2023-04-05, 最終更新日: 2024-02-07)
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: 37012377
DOI: 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)
構造検証レポート
Validation report summary of 8ag8
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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