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Artículo

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

Otero, Lisandro HoracioIcon ; Foscaldi, Sabrina AndreaIcon ; Antelo, Giuliano TomásIcon ; Rosano, German LeandroIcon ; Sirigu, Serena; Klinke, SebastianIcon ; Defelipe, Lucas AlfredoIcon ; Sánchez Lamas, Maximiliano; Battocchio, Giovanni; Conforte, Valeria PaolaIcon ; Vojnov, Adrián AlbertoIcon ; Chavas, Leonard M.G.; Goldbaum, Fernando AlbertoIcon ; Mroginski, Maria Andrea; Rinaldi, Jimena JulietaIcon ; Bonomi, Hernán RuyIcon
Fecha de publicación: 11/2021
Editorial: American Association for the Advancement of Science
Revista: Science Advances
e-ISSN: 2375-2548
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Biofísica

Resumen

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 XccBphP 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.
Palabras clave: Phytochrome , Biliverdine , X-ray crystallography
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial 2.5 Unported (CC BY-NC 2.5)
Identificadores
URI: http://hdl.handle.net/11336/167152
DOI: http://dx.doi.org/10.1126/sciadv.abh1097
URL: https://www.science.org/doi/10.1126/sciadv.abh1097
Colecciones
Articulos(IBR)
Articulos de INST.DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Articulos(ICT - MILSTEIN)
Articulos de INST.DE CS. Y TECNOLOGIA "DR. CESAR MILSTEIN"
Articulos(IIBBA)
Articulos de INST.DE INVEST.BIOQUIMICAS DE BS.AS(I)
Citación
Otero, Lisandro Horacio; Foscaldi, Sabrina Andrea; Antelo, Giuliano Tomás; Rosano, German Leandro; Sirigu, Serena; et al.; Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level; American Association for the Advancement of Science; Science Advances; 7; 48; 11-2021; 1-22
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