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  Structure of a bacterial BLUF photoreceptor: insights into blue light-mediated signal transduction

Jung, A., Domratcheva, T., Tarutina, M., Wu, Q., Ko, W.-H., Shoeman, R. L., et al. (2005). Structure of a bacterial BLUF photoreceptor: insights into blue light-mediated signal transduction. Proceedings of the National Academy of Sciences of the United States of America, 102(35), 12350-12355. doi:10.1073/pnas.0500722102.

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Genre: Journal Article
Alternative Title : Structure of a bacterial BLUF photoreceptor: insights into blue light-mediated signal transduction

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PNAS_102_2005_12350.pdf (Any fulltext), 315KB
 
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 Creators:
Jung, Astrid1, Author              
Domratcheva, Tatjana, Author
Tarutina, Marina, Author
Wu, Qiong, Author
Ko, Wen-Huang, Author
Shoeman, Robert L.1, Author              
Gomelsky, Mark1, Author              
Gardner, Kevin H., Author
Schlichting, Ilme1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: blue light sensing, photochemistry, protein function, flavin, reaction mechanism
 Abstract: Light is an essential environmental factor, and many species have evolved the capability to respond to it. Blue light is perceived through three flavin-containing photoreceptor families: cryptochromes, light-oxygen-voltage, and BLUF (sensor of blue light using flavin adenine dinucleotide, FAD) domain proteins. BLUF domains are present in various proteins from Bacteria and lower Eukarya. They are fully modular and can relay signals to structurally and functionally diverse output units, most of which are implicated in nucleotide metabolism. We present the high resolution crystal structure of the dark resting state of BlrB, a short BLUF domain-containing protein from Rhodobacter sphaeroides. The structure reveals a previously uncharacterized FAD-binding fold. Along with other lines of evidence, it suggests mechanistic aspects for the photocycle that is characterized by a red-shifted absorbance of the flavin. The isoalloxazine ring of FAD binds in a cleft between two helices, whereas the adenine ring points into the solvent. We propose that the adenine ring serves as a hook mediating the interaction with its effector/output domain. The structure suggests a unique photochemical signaling switch in which the absorption of light induces a structural change in the rim surrounding the hook, thereby changing the protein interface between BLUF and the output domain.

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Language(s): eng - English
 Dates: 2005-01-272005-08-172005-08-172005-08-30
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: National Academy of Sciences
Pages: - Volume / Issue: 102 (35) Sequence Number: - Start / End Page: 12350 - 12355 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230