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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...
Autores principales: | , , , , , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Crystallographic Association
2019
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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. |
format | Online Article Text |
id | pubmed-6748860 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | American Crystallographic Association |
record_format | MEDLINE/PubMed |
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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