Biological Sciences Division
Published May 27, 2022 | Version v1
Journal article Open

Light-induced protein structural dynamics in bacteriophytochrome revealed by time-resolved x-ray solution scattering

Creators

  • 1. Korea Advanced Institute of Science and Technology
  • 2. Mokpo National University
  • 3. University of Illinois at Chicago
  • 4. University of Chicago

Description

Bacteriophytochromes (BphPs) are photoreceptors that regulate a wide range of biological mechanisms via red light–absorbing (Pr)–to–far-red light–absorbing (Pfr) reversible photoconversion. The structural dynamics underlying Pfr-to-Pr photoconversion in a liquid solution phase are not well understood. We used time-resolved x-ray solution scattering (TRXSS) to capture light-induced structural transitions in the bathy BphP photosensory module of Pseudomonas aeruginosa. Kinetic analysis of the TRXSS data identifies three distinct structural species, which are attributed to lumi-F, meta-F, and Pr, connected by time constants of 95 μs and 21 ms. Structural analysis based on molecular dynamics simulations shows that the light activation of PaBphP accompanies quaternary structural rearrangements from an "II"-framed close form of the Pfr state to an "O"-framed open form of the Pr state in terms of the helical backbones. This study provides mechanistic insights into how modular signaling proteins such as BphPs transmit structural signals over long distances and regulate their downstream biological responses.

Data availability

All data needed to evaluate the conclusions in the paper are present in the paper and/or the Supplementary Materials.

Files

sciadv.abm6278.pdf

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Additional details

Identifiers

DOI
10.1126/sciadv.abm6278
Other
oai:uchicago.tind.io:10921

Funding

U.S. Department of Energy
DE-AC02-06CH11357
Institute for Basic Science
IBS-R033
National Institutes of Health
GM036452
National Institutes of Health
EY024363
National Institutes of Health National Institute of General Medical Sciences
R24GM111072

UChicago Information

Division(s)
Biological Sciences Division
Department(s)
Biochemistry and Molecular Biology