Mutational Study of the Tryptophan Tetrad Important for Electron Transfer in European Robin Cryptochrome 4a.

Autor:	Frederiksen A; Institute of Physics, Carl von Ossietzky Universität Oldenburg, Carl-von-Ossietzky Strasse 9-11, Oldenburg 26129, Germany., Langebrake C; Institute of Avian Research, An der Vogelwarte 21, Wilhelmshaven 26386, Germany., Hanić M; Institute of Physics, Carl von Ossietzky Universität Oldenburg, Carl-von-Ossietzky Strasse 9-11, Oldenburg 26129, Germany., Manthey G; Institute of Physics, Carl von Ossietzky Universität Oldenburg, Carl-von-Ossietzky Strasse 9-11, Oldenburg 26129, Germany.; Institute of Avian Research, An der Vogelwarte 21, Wilhelmshaven 26386, Germany., Mouritsen H; Department of Biology and Environmental Sciences, Carl von Ossietzky University of Oldenburg, Carl-von-Ossietzky Strasse 9-11, Oldenburg 26129, Germany.; Research Centre for Neurosensory Sciences, Carl von Ossietzky University of Oldenburg, Carl-von-Ossietzky Strasse 9-11, Oldenburg 26129, Germany., Liedvogel M; Institute of Avian Research, An der Vogelwarte 21, Wilhelmshaven 26386, Germany.; Department of Biology and Environmental Sciences, Carl von Ossietzky University of Oldenburg, Carl-von-Ossietzky Strasse 9-11, Oldenburg 26129, Germany.; MPRG Behavioural Genomics, Max Planck Institute for Evolutionary Biology, August-Thienemann-Str. 2, Plön 24306, Germany., Solov'yov IA; Institute of Physics, Carl von Ossietzky Universität Oldenburg, Carl-von-Ossietzky Strasse 9-11, Oldenburg 26129, Germany.; Research Centre for Neurosensory Sciences, Carl von Ossietzky University of Oldenburg, Carl-von-Ossietzky Strasse 9-11, Oldenburg 26129, Germany.; Department of Physics, Center for Nanoscale Dynamics (CENAD), Carl von Ossietzky University of Oldenburg, Ammerländer Heerstr. 114-118, Oldenburg 26129, Germany.
Jazyk:	angličtina
Zdroj:	ACS omega [ACS Omega] 2023 Jul 12; Vol. 8 (29), pp. 26425-26436. Date of Electronic Publication: 2023 Jul 12 (Print Publication: 2023).
DOI:	10.1021/acsomega.3c02963
Abstrakt:	The ability of migratory birds to sense magnetic fields has been known for decades, although the understanding of the underlying mechanism is still elusive. Currently, the strongest magnetoreceptor candidate in birds is a protein called cryptochrome 4a. The cryptochrome 4a protein has changed through evolution, apparently endowing some birds with a more pronounced magnetic sensitivity than others. Using phylogenetic tools, we show that a specific tryptophan tetrad and a tyrosine residue predicted to be essential for cryptochrome activation are highly conserved in the avian clade. Through state-of-the-art molecular dynamics simulations and associated analyses, we also studied the role of these specific residues and the associated mutants on the overall dynamics of the protein. The analyses of the single residue mutations were used to judge how far a local change in the protein structure can impact specific dynamics of European robin cryptochrome 4a. We conclude that the replacements of each of the tryptophans one by one with a phenylalanine do not compromise the overall stability of the protein. Competing Interests: The authors declare no competing financial interest. (© 2023 The Authors. Published by American Chemical Society.)
Databáze:	MEDLINE
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