Crystal structure of a bacterial photoactivated adenylate cyclase determined by serial femtosecond and serial synchrotron crystallography Article Swipe
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· 2024
· Open Access
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· DOI: https://doi.org/10.1107/s2052252524010170
OaPAC is a recently discovered blue-light-using flavin adenosine dinucleotide (BLUF) photoactivated adenylate cyclase from the cyanobacterium Oscillatoria acuminata that uses adenosine triphosphate and translates the light signal into the production of cyclic adenosine monophosphate. Here, we report crystal structures of the enzyme in the absence of its natural substrate determined from room-temperature serial crystallography data collected at both an X-ray free-electron laser and a synchrotron, and we compare these structures with cryo-macromolecular crystallography structures obtained at a synchrotron by us and others. These results reveal slight differences in the structure of the enzyme due to data collection at different temperatures and X-ray sources. We further investigate the effect of the Y6W mutation in the BLUF domain, a mutation which results in a rearrangement of the hydrogen-bond network around the flavin and a notable rotation of the side chain of the critical Gln48 residue. These studies pave the way for picosecond–millisecond time-resolved serial crystallography experiments at X-ray free-electron lasers and synchrotrons in order to determine the early structural intermediates and correlate them with the well studied picosecond–millisecond spectroscopic intermediates.
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- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1107/s2052252524010170
- OA Status
- gold
- Cited By
- 3
- References
- 86
- Related Works
- 10
- OpenAlex ID
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Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4403851545Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1107/s2052252524010170Digital Object Identifier
- Title
-
Crystal structure of a bacterial photoactivated adenylate cyclase determined by serial femtosecond and serial synchrotron crystallographyWork title
- Type
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articleOpenAlex work type
- Language
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enPrimary language
- Publication year
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2024Year of publication
- Publication date
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2024-10-29Full publication date if available
- Authors
-
Sofia M. Kapetanaki, Nicolas Coquelle, David von Stetten, Martin Byrdin, Ronald Rios-Santacruz, Richard Bean, Johan Bielecki, Mohamed Boudjelida, Zsuzsanna Fekete, G.W. Grime, Huijong Han, Caitlin Hatton, Sravya Kantamneni, Konstantin Kharitonov, Chan Kim, Marco Kloos, F. Koua, Iñaki de Diego, Diogo V. M. Melo, Lukas Rane, Adam Round, Ekaterina Round, Abhisakh Sarma, Robin Schubert, Joachim Schulz, Marcin Sikorski, Mohammad Vakili, Joana Valério, Jovana Vitas, Raphaël de Wijn, Agnieszka Wrona, Ninon Zala, Arwen R. Pearson, Katerina Dörner, Giorgio Schirò, Elspeth F. Garman, András Lukács, Martin H. WeikList of authors in order
- Landing page
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https://doi.org/10.1107/s2052252524010170Publisher landing page
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YesWhether a free full text is available
- OA status
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goldOpen access status per OpenAlex
- OA URL
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https://doi.org/10.1107/s2052252524010170Direct OA link when available
- Concepts
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Chemistry, Flavin adenine dinucleotide, Crystallography, Femtosecond, Synchrotron, Crystal structure, Laser, Enzyme, Cofactor, Biochemistry, Physics, OpticsTop concepts (fields/topics) attached by OpenAlex
- Cited by
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3Total citation count in OpenAlex
- Citations by year (recent)
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2025: 3Per-year citation counts (last 5 years)
- References (count)
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86Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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