Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level.

Autor:	Otero LH; Fundación Instituto Leloir, IIBBA-CONICET, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina.; Plataforma Argentina de Biología Estructural y Metabolómica PLABEM, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina., Foscaldi S; Fundación Instituto Leloir, IIBBA-CONICET, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina., Antelo GT; Fundación Instituto Leloir, IIBBA-CONICET, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina., Rosano GL; Unidad de Espectrometría de Masa, Instituto de Biología Molecular y Celular de Rosario, UEM-IBR, CONICET, Bv. 27 de Febrero (S2000EZP), Rosario, Argentina., Sirigu S; Proxima-1, Synchrotron SOLEIL, L'Orme des Merisiers, Saint-Aubin, BP 48 (91192), Gif-sur-Yvette Cedex, France., Klinke S; Fundación Instituto Leloir, IIBBA-CONICET, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina.; Plataforma Argentina de Biología Estructural y Metabolómica PLABEM, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina., Defelipe LA; European Molecular Biology Laboratory (EMBL), Hamburg Unit, Notkestrasse 85 (22607), Hamburg, Germany., Sánchez-Lamas M; Fundación Instituto Leloir, IIBBA-CONICET, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina., Battocchio G; Technische Universität Berlin, Institute of Chemistry, Strasse des 17. Juni 135 (D-10623), Berlin, Germany., Conforte V; Instituto de Ciencia y Tecnología Dr. César Milstein, Fundación Pablo Cassará, CONICET, Saladillo 2468 (C1440FFX), Buenos Aires, Argentina., Vojnov AA; Instituto de Ciencia y Tecnología Dr. César Milstein, Fundación Pablo Cassará, CONICET, Saladillo 2468 (C1440FFX), Buenos Aires, Argentina., Chavas LMG; Proxima-1, Synchrotron SOLEIL, L'Orme des Merisiers, Saint-Aubin, BP 48 (91192), Gif-sur-Yvette Cedex, France.; Synchrotron Radiation Research Center, Nagoya University, Nagoya 464-8603, Japan., Goldbaum FA; Fundación Instituto Leloir, IIBBA-CONICET, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina.; Plataforma Argentina de Biología Estructural y Metabolómica PLABEM, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina., Mroginski MA; Technische Universität Berlin, Institute of Chemistry, Strasse des 17. Juni 135 (D-10623), Berlin, Germany., Rinaldi J; Fundación Instituto Leloir, IIBBA-CONICET, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina., Bonomi HR; Fundación Instituto Leloir, IIBBA-CONICET, Av. Patricias Argentinas 435 (C1405BWE), Buenos Aires, Argentina.
Jazyk:	angličtina
Zdroj:	Science advances [Sci Adv] 2021 Nov 26; Vol. 7 (48), pp. eabh1097. Date of Electronic Publication: 2021 Nov 24.
DOI:	10.1126/sciadv.abh1097
Abstrakt:	Phytochromes constitute a widespread photoreceptor family that typically interconverts between two photostates called Pr (red light–absorbing) and Pfr (far-red light–absorbing). The lack of full-length structures solved at the (near-)atomic level in both pure Pr and Pfr states leaves gaps in the structural mechanisms involved in the signal transmission pathways during the photoconversion. Here, we present the crystallographic structures of three versions from the plant pathogen Xanthomonas campestris virulence regulator Xcc 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.
Databáze:	MEDLINE
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