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  • Amino Acid Substitution  (1)
  • American Association for the Advancement of Science (AAAS)  (1)
  • National Academy of Sciences
  • 2005-2009  (1)
  • 1965-1969
  • 1940-1944
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  • American Association for the Advancement of Science (AAAS)  (1)
  • National Academy of Sciences
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  • 2005-2009  (1)
  • 1965-1969
  • 1940-1944
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    Publikationsdatum: 2007-05-19
    Beschreibung: The Neurospora crassa photoreceptor Vivid tunes blue-light responses and modulates gating of the circadian clock. Crystal structures of dark-state and light-state Vivid reveal a light, oxygen, or voltage Per-Arnt-Sim domain with an unusual N-terminal cap region and a loop insertion that accommodates the flavin cofactor. Photoinduced formation of a cystein-flavin adduct drives flavin protonation to induce an N-terminal conformational change. A cysteine-to-serine substitution remote from the flavin adenine dinucleotide binding site decouples conformational switching from the flavin photocycle and prevents Vivid from sending signals in Neurospora. Key elements of this activation mechanism are conserved by other photosensors such as White Collar-1, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1 (FKF1).〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3682417/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3682417/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zoltowski, Brian D -- Schwerdtfeger, Carsten -- Widom, Joanne -- Loros, Jennifer J -- Bilwes, Alexandrine M -- Dunlap, Jay C -- Crane, Brian R -- GM079879-01/GM/NIGMS NIH HHS/ -- MH44651/MH/NIMH NIH HHS/ -- P01 GM068087/GM/NIGMS NIH HHS/ -- R01 GM034985/GM/NIGMS NIH HHS/ -- R01 GM034985-24/GM/NIGMS NIH HHS/ -- R37GM34985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 May 18;316(5827):1054-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17510367" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adaptation, Physiological ; Amino Acid Sequence ; Amino Acid Substitution ; Binding Sites ; Crystallography, X-Ray ; Darkness ; Dimerization ; Flavin-Adenine Dinucleotide/chemistry ; Fungal Proteins/*chemistry/genetics/metabolism ; Light ; Molecular Sequence Data ; Mutagenesis ; Neurospora crassa/*chemistry ; Protein Conformation ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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