Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level
Lisandro H. Otero, Sabrina Foscaldi, Giuliano T. Antelo, Germán L. Rosano, Serena Sirigu, Sebastián Klinke, Lucas A. Defelipe, Maximiliano Sánchez‐Lamas, Giovanni Battocchio, Valeria P. Conforte, Adrián A. Vojnov, Leonard M. G. Chavas, Fernando A. Goldbaum, María Andrea Mroginski, Jimena Rinaldi, Hernán R. Bonomi
Abstract
BphP bacteriophytochrome, including two full-length proteins, in the Pr and Pfr states. The structures show a reorganization of the interaction networks within and around the chromophore-binding pocket, an α-helix/β-sheet tongue transition, and specific domain reorientations, along with interchanging kinks and breaks at the helical spine as a result of the photoswitching, which subsequently affect the quaternary assembly. These structural findings, combined with multidisciplinary studies, allow us to describe the signaling mechanism of a full-length bacterial phytochrome at the atomic level.