ArticleBiophysical journal2012
pH dependence of the photoactive yellow protein photocycle investigated by time-resolved crystallography.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 44 citations in OpenAlex.
- Article
- The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- Watching a signaling protein function: What has been learned over four decades of time-resolved studies of photoactive yellow protein.Structural dynamics (Melville, N.Y.) · 2024Review
- Practical considerations for the analysis of time-resolved x-ray data.Structural dynamics (Melville, N.Y.) · 2023Article
- Emerging Time-Resolved X-Ray Diffraction Approaches for Protein Dynamics.Annual review of biophysics · 2023Review
- Biological function investigated by time-resolved structure determination.Structural dynamics (Melville, N.Y.) · 2023Article
- A unifying Bayesian framework for merging X-ray diffraction data.Nature communications · 2022Article
- Article
- Serial Crystallography for Structure-Based Drug Discovery.Trends in pharmacological sciences · 2020Review
- Time-resolved serial femtosecond crystallography at the European XFEL.Nature methods · 2020Article
- Time-Resolved Macromolecular Crystallography at Pulsed X-ray Sources.International journal of molecular sciences · 2019Review
- Capturing the photo-signaling state of a photoreceptor in a steady-state fashion by binding a transition metal complex.Protein science : a publication of the Protein Society · 2017Article
- Watching Proteins Function with Time-resolved X-ray Crystallography.Journal of physics D: Applied physics · 2017Article
- Developing HIV-1 Protease Inhibitors through Stereospecific Reactions in Protein Crystals.Molecules (Basel, Switzerland) · 2016Article
- Graphene-based microfluidics for serial crystallography.Lab on a chip · 2016Article
- Towards time-resolved serial crystallography in a microfluidic device.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Perspective: On the relevance of slower-than-femtosecond time scales in chemical structural-dynamics studies.Structural dynamics (Melville, N.Y.) · 2015Article
- A split-beam probe-pump-probe scheme for femtosecond time resolved protein X-ray crystallography.Structural dynamics (Melville, N.Y.) · 2015Article
- Reply to 'contradictions in X-ray structures of intermediates in the photocycle of photoactive yellow protein'.Nature chemistry · 2014Article
- Probing anisotropic structure changes in proteins with picosecond time-resolved small-angle X-ray scattering.The journal of physical chemistry. B · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Visualizing the three-dimensional structures of a protein during its biological activity is key to understanding its mechanism. In general, protein structure and function are pH-dependent. Changing the pH provides new insights into the mechanisms that are involved in protein activity. Photoactive yellow protein (PYP) is a signaling protein that serves as an ideal model for time-dependent studies on light-activated proteins. Its photocycle is studied extensively under different pH conditions. However, the structures of the intermediates remain unknown until time-resolved crystallography is employed. With the newest beamline developments, a comprehensive time series of Laue data can now be collected from a single protein crystal. This allows us to vary the pH. Here we present the first structure, to our knowledge, of a short-lived protein-inhibitor complex formed in the pB state of the PYP photocycle at pH 4. A water molecule that is transiently stabilized in the chromophore active site prevents the relaxation of the chromophore back to the trans configuration. As a result, the dark-state recovery is slowed down dramatically. At pH 9, PYP stops cycling through the pB state altogether. The electrostatic environment in the chromophore-binding site is the likely reason for this altered kinetics at different pH values.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.