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High-resolution crystal structures of a myxobacterial phytochrome at cryo and room temperatures

Phytochromes (PHYs) are photoreceptor proteins first discovered in plants, where they control a variety of photomorphogenesis events. PHYs as photochromic proteins can reversibly switch between two distinct states: a red light (Pr) and a far-red light (Pfr) absorbing form. The discovery of Bacteriop...

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Autores principales: Sanchez, Juan C., Carrillo, Melissa, Pandey, Suraj, Noda, Moraima, Aldama, Luis, Feliz, Denisse, Claesson, Elin, Wahlgren, Weixiao Yuan, Tracy, Gregory, Duong, Phu, Nugent, Angela C., Field, Andrew, Šrajer, Vukica, Kupitz, Christopher, Iwata, So, Nango, Eriko, Tanaka, Rie, Tanaka, Tomoyuki, Fangjia, Luo, Tono, Kensuke, Owada, Shigeki, Westenhoff, Sebastian, Schmidt, Marius, Stojković, Emina A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Crystallographic Association 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6748860/
https://www.ncbi.nlm.nih.gov/pubmed/31559319
http://dx.doi.org/10.1063/1.5120527
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author Sanchez, Juan C.
Carrillo, Melissa
Pandey, Suraj
Noda, Moraima
Aldama, Luis
Feliz, Denisse
Claesson, Elin
Wahlgren, Weixiao Yuan
Tracy, Gregory
Duong, Phu
Nugent, Angela C.
Field, Andrew
Šrajer, Vukica
Kupitz, Christopher
Iwata, So
Nango, Eriko
Tanaka, Rie
Tanaka, Tomoyuki
Fangjia, Luo
Tono, Kensuke
Owada, Shigeki
Westenhoff, Sebastian
Schmidt, Marius
Stojković, Emina A.
author_facet Sanchez, Juan C.
Carrillo, Melissa
Pandey, Suraj
Noda, Moraima
Aldama, Luis
Feliz, Denisse
Claesson, Elin
Wahlgren, Weixiao Yuan
Tracy, Gregory
Duong, Phu
Nugent, Angela C.
Field, Andrew
Šrajer, Vukica
Kupitz, Christopher
Iwata, So
Nango, Eriko
Tanaka, Rie
Tanaka, Tomoyuki
Fangjia, Luo
Tono, Kensuke
Owada, Shigeki
Westenhoff, Sebastian
Schmidt, Marius
Stojković, Emina A.
author_sort Sanchez, Juan C.
collection PubMed
description Phytochromes (PHYs) are photoreceptor proteins first discovered in plants, where they control a variety of photomorphogenesis events. PHYs as photochromic proteins can reversibly switch between two distinct states: a red light (Pr) and a far-red light (Pfr) absorbing form. The discovery of Bacteriophytochromes (BphPs) in nonphotosynthetic bacteria has opened new frontiers in our understanding of the mechanisms by which these natural photoswitches can control single cell development, although the role of BphPs in vivo remains largely unknown. BphPs are dimeric proteins that consist of a photosensory core module (PCM) and an enzymatic domain, often a histidine kinase. The PCM is composed of three domains (PAS, GAF, and PHY). It holds a covalently bound open-chain tetrapyrrole (biliverdin, BV) chromophore. Upon absorption of light, the double bond between BV rings C and D isomerizes and reversibly switches the protein between Pr and Pfr states. We report crystal structures of the wild-type and mutant (His275Thr) forms of the canonical BphP from the nonphotosynthetic myxobacterium Stigmatella aurantiaca (SaBphP2) in the Pr state. Structures were determined at 1.65 Å and 2.2 Å (respectively), the highest resolution of any PCM construct to date. We also report the room temperature wild-type structure of the same protein determined at 2.1 Å at the SPring-8 Angstrom Compact free electron LAser (SACLA), Japan. Our results not only highlight and confirm important amino acids near the chromophore that play a role in Pr-Pfr photoconversion but also describe the signal transduction into the PHY domain which moves across tens of angstroms after the light stimulus.
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spelling pubmed-67488602019-09-26 High-resolution crystal structures of a myxobacterial phytochrome at cryo and room temperatures Sanchez, Juan C. Carrillo, Melissa Pandey, Suraj Noda, Moraima Aldama, Luis Feliz, Denisse Claesson, Elin Wahlgren, Weixiao Yuan Tracy, Gregory Duong, Phu Nugent, Angela C. Field, Andrew Šrajer, Vukica Kupitz, Christopher Iwata, So Nango, Eriko Tanaka, Rie Tanaka, Tomoyuki Fangjia, Luo Tono, Kensuke Owada, Shigeki Westenhoff, Sebastian Schmidt, Marius Stojković, Emina A. Struct Dyn ARTICLES Phytochromes (PHYs) are photoreceptor proteins first discovered in plants, where they control a variety of photomorphogenesis events. PHYs as photochromic proteins can reversibly switch between two distinct states: a red light (Pr) and a far-red light (Pfr) absorbing form. The discovery of Bacteriophytochromes (BphPs) in nonphotosynthetic bacteria has opened new frontiers in our understanding of the mechanisms by which these natural photoswitches can control single cell development, although the role of BphPs in vivo remains largely unknown. BphPs are dimeric proteins that consist of a photosensory core module (PCM) and an enzymatic domain, often a histidine kinase. The PCM is composed of three domains (PAS, GAF, and PHY). It holds a covalently bound open-chain tetrapyrrole (biliverdin, BV) chromophore. Upon absorption of light, the double bond between BV rings C and D isomerizes and reversibly switches the protein between Pr and Pfr states. We report crystal structures of the wild-type and mutant (His275Thr) forms of the canonical BphP from the nonphotosynthetic myxobacterium Stigmatella aurantiaca (SaBphP2) in the Pr state. Structures were determined at 1.65 Å and 2.2 Å (respectively), the highest resolution of any PCM construct to date. We also report the room temperature wild-type structure of the same protein determined at 2.1 Å at the SPring-8 Angstrom Compact free electron LAser (SACLA), Japan. Our results not only highlight and confirm important amino acids near the chromophore that play a role in Pr-Pfr photoconversion but also describe the signal transduction into the PHY domain which moves across tens of angstroms after the light stimulus. American Crystallographic Association 2019-09-17 /pmc/articles/PMC6748860/ /pubmed/31559319 http://dx.doi.org/10.1063/1.5120527 Text en © 2019 Author(s). 2329-7778/2019/6(5)/054701/9 All article content, except where otherwise noted, is licensed under a Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle ARTICLES
Sanchez, Juan C.
Carrillo, Melissa
Pandey, Suraj
Noda, Moraima
Aldama, Luis
Feliz, Denisse
Claesson, Elin
Wahlgren, Weixiao Yuan
Tracy, Gregory
Duong, Phu
Nugent, Angela C.
Field, Andrew
Šrajer, Vukica
Kupitz, Christopher
Iwata, So
Nango, Eriko
Tanaka, Rie
Tanaka, Tomoyuki
Fangjia, Luo
Tono, Kensuke
Owada, Shigeki
Westenhoff, Sebastian
Schmidt, Marius
Stojković, Emina A.
High-resolution crystal structures of a myxobacterial phytochrome at cryo and room temperatures
title High-resolution crystal structures of a myxobacterial phytochrome at cryo and room temperatures
title_full High-resolution crystal structures of a myxobacterial phytochrome at cryo and room temperatures
title_fullStr High-resolution crystal structures of a myxobacterial phytochrome at cryo and room temperatures
title_full_unstemmed High-resolution crystal structures of a myxobacterial phytochrome at cryo and room temperatures
title_short High-resolution crystal structures of a myxobacterial phytochrome at cryo and room temperatures
title_sort high-resolution crystal structures of a myxobacterial phytochrome at cryo and room temperatures
topic ARTICLES
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6748860/
https://www.ncbi.nlm.nih.gov/pubmed/31559319
http://dx.doi.org/10.1063/1.5120527
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