Ubiquitous Structural Signaling in Bacterial Phytochromes.
(2015) In The Journal of Physical Chemistry Letters 6(17). p.3379-3383- Abstract
- The phytochrome family of light-switchable proteins has long been studied by biochemical, spectroscopic and crystallographic means, while a direct probe for global conformational signal propagation has been lacking. Using solution X-ray scattering, we find that the photosensory cores of several bacterial phytochromes undergo similar large-scale structural changes upon red-light excitation. The data establish that phytochromes with ordinary and inverted photocycles share a structural signaling mechanism and that a particular conserved histidine, previously proposed to be involved in signal propagation, in fact tunes photoresponse.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/7841023
- author
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- The Journal of Physical Chemistry Letters
- volume
- 6
- issue
- 17
- pages
- 3379 - 3383
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:26275765
- wos:000360953300010
- pmid:26275765
- scopus:84942606333
- ISSN
- 1948-7185
- DOI
- 10.1021/acs.jpclett.5b01629
- language
- English
- LU publication?
- yes
- id
- a14602b1-2bee-48f7-8ae5-3461da664bd9 (old id 7841023)
- date added to LUP
- 2016-04-01 13:25:56
- date last changed
- 2022-02-19 05:27:57
@article{a14602b1-2bee-48f7-8ae5-3461da664bd9, abstract = {{The phytochrome family of light-switchable proteins has long been studied by biochemical, spectroscopic and crystallographic means, while a direct probe for global conformational signal propagation has been lacking. Using solution X-ray scattering, we find that the photosensory cores of several bacterial phytochromes undergo similar large-scale structural changes upon red-light excitation. The data establish that phytochromes with ordinary and inverted photocycles share a structural signaling mechanism and that a particular conserved histidine, previously proposed to be involved in signal propagation, in fact tunes photoresponse.}}, author = {{Björling, Alexander and Berntsson, Oskar and Takala, Heikki and Gallagher, Kevin D and Patel, Hardik and Gustavsson, Emil and St Peter, Rachael and Duong, Phu and Nugent, Angela and Zhang, Fan and Berntsen, Peter and Appio, Roberto and Rajkovic, Ivan and Lehtivuori, Heli and Panman, Matthijs R and Hoernke, Maria and Niebling, Stephan and Harimoorthy, Rajiv and Lamparter, Tilman and Stojković, Emina A and Ihalainen, Janne A and Westenhoff, Sebastian}}, issn = {{1948-7185}}, language = {{eng}}, number = {{17}}, pages = {{3379--3383}}, publisher = {{The American Chemical Society (ACS)}}, series = {{The Journal of Physical Chemistry Letters}}, title = {{Ubiquitous Structural Signaling in Bacterial Phytochromes.}}, url = {{http://dx.doi.org/10.1021/acs.jpclett.5b01629}}, doi = {{10.1021/acs.jpclett.5b01629}}, volume = {{6}}, year = {{2015}}, }