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

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 str...

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Autores principales: Otero, Lisandro H., Foscaldi, Sabrina, Antelo, Giuliano T., Rosano, Germán L., Sirigu, Serena, Klinke, Sebastián, Defelipe, Lucas A., Sánchez-Lamas, Maximiliano, Battocchio, Giovanni, Conforte, Valeria, Vojnov, Adrián A., Chavas, Leonard M. G., Goldbaum, Fernando A., Mroginski, Maria-Andrea, Rinaldi, Jimena, Bonomi, Hernán R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8612531/
https://www.ncbi.nlm.nih.gov/pubmed/34818032
http://dx.doi.org/10.1126/sciadv.abh1097
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author Otero, Lisandro H.
Foscaldi, Sabrina
Antelo, Giuliano T.
Rosano, Germán L.
Sirigu, Serena
Klinke, Sebastián
Defelipe, Lucas A.
Sánchez-Lamas, Maximiliano
Battocchio, Giovanni
Conforte, Valeria
Vojnov, Adrián A.
Chavas, Leonard M. G.
Goldbaum, Fernando A.
Mroginski, Maria-Andrea
Rinaldi, Jimena
Bonomi, Hernán R.
author_facet Otero, Lisandro H.
Foscaldi, Sabrina
Antelo, Giuliano T.
Rosano, Germán L.
Sirigu, Serena
Klinke, Sebastián
Defelipe, Lucas A.
Sánchez-Lamas, Maximiliano
Battocchio, Giovanni
Conforte, Valeria
Vojnov, Adrián A.
Chavas, Leonard M. G.
Goldbaum, Fernando A.
Mroginski, Maria-Andrea
Rinaldi, Jimena
Bonomi, Hernán R.
author_sort Otero, Lisandro H.
collection PubMed
description 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.
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spelling pubmed-86125312021-12-06 Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level Otero, Lisandro H. Foscaldi, Sabrina Antelo, Giuliano T. Rosano, Germán L. Sirigu, Serena Klinke, Sebastián Defelipe, Lucas A. Sánchez-Lamas, Maximiliano Battocchio, Giovanni Conforte, Valeria Vojnov, Adrián A. Chavas, Leonard M. G. Goldbaum, Fernando A. Mroginski, Maria-Andrea Rinaldi, Jimena Bonomi, Hernán R. Sci Adv Biomedicine and Life Sciences 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. American Association for the Advancement of Science 2021-11-24 /pmc/articles/PMC8612531/ /pubmed/34818032 http://dx.doi.org/10.1126/sciadv.abh1097 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.
spellingShingle Biomedicine and Life Sciences
Otero, Lisandro H.
Foscaldi, Sabrina
Antelo, Giuliano T.
Rosano, Germán L.
Sirigu, Serena
Klinke, Sebastián
Defelipe, Lucas A.
Sánchez-Lamas, Maximiliano
Battocchio, Giovanni
Conforte, Valeria
Vojnov, Adrián A.
Chavas, Leonard M. G.
Goldbaum, Fernando A.
Mroginski, Maria-Andrea
Rinaldi, Jimena
Bonomi, Hernán R.
Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level
title Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level
title_full Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level
title_fullStr Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level
title_full_unstemmed Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level
title_short Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level
title_sort structural basis for the pr-pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level
topic Biomedicine and Life Sciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8612531/
https://www.ncbi.nlm.nih.gov/pubmed/34818032
http://dx.doi.org/10.1126/sciadv.abh1097
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