9F1Z

Crystal structure of adenylyate cyclase variant Y6W

Summary for 9F1Z

• Entry DOI: 10.2210/pdb9f1z/pdb
• Descriptor: Family 3 adenylate cyclase, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: fad, mutant, y6w, adenylate cyclase, lyase
• Biological source: Oscillatoria acuminata
• Total number of polymer chains: 1
• Total formula weight: 40001.53

Authors

Kapetanaki, S.,Coquelle, N.,Weik, M. (deposition date: 2024-04-20, release date: 2025-02-26, Last modification date: 2025-03-19)

Primary citation

Kapetanaki, S.M.,Coquelle, N.,von Stetten, D.,Byrdin, M.,Rios-Santacruz, R.,Bean, R.,Bielecki, J.,Boudjelida, M.,Fekete, Z.,Grime, G.W.,Han, H.,Hatton, C.,Kantamneni, S.,Kharitonov, K.,Kim, C.,Kloos, M.,Koua, F.H.M.,de Diego Martinez, I.,Melo, D.,Rane, L.,Round, A.,Round, E.,Sarma, A.,Schubert, R.,Schulz, J.,Sikorski, M.,Vakili, M.,Valerio, J.,Vitas, J.,de Wijn, R.,Wrona, A.,Zala, N.,Pearson, A.,Dorner, K.,Schiro, G.,Garman, E.F.,Lukacs, A.,Weik, M.
Crystal structure of a bacterial photoactivated adenylate cyclase determined by serial femtosecond and serial synchrotron crystallography.
Iucrj, 11:991-1006, 2024

PubMed Abstract: 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.

PubMed: 39470573
DOI: 10.1107/S2052252524010170

Experimental method

X-RAY DIFFRACTION (1.95 Å)