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  Glutamine Amide Flip Elicits Long Distance Allosteric Responses in the LOV Protein Vivid

Ganguly, A., Thiel, W., & Crane, B. R. (2017). Glutamine Amide Flip Elicits Long Distance Allosteric Responses in the LOV Protein Vivid. Journal of the American Chemical Society, 139(8), 2972-2980. doi:10.1021/jacs.6b10701.

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Ganguly, Abir1, Author              
Thiel, Walter1, Author              
Crane, Brian R.2, Author
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1Research Department Thiel, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445590              
2Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States, ou_persistent22              

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 Abstract: Light-oxygen-voltage (LOV) domains sense blue light through the photochemical formation of a cysteinyl-flavin covalent adduct. Concurrent protonation at the flavin N5 position alters the hydrogen bonding interactions of an invariant Gln residue that has been proposed to flip its amide side chain as a critical step in the propagation of conformational change. Traditional molecular dynamics (MD) and replica-exchange MD (REMD) simulations of the well-characterized LOV protein Vivid (VVD) demonstrate that the Gln182 amide indeed reorients by ∼180° in response to either adduct formation or reduction of the isoalloxazine ring to the neutral semiquinone, both of which involve N5 protonation. Free energy simulations reveal that the relative free energies of the flipped Gln conformation and the flipping barrier are significantly lower in the light-adapted state. The Gln182 flip stabilizes an important hinge-bβ region between the PAS β-sheet and the N-terminal cap helix that in turn destabilizes an N-terminal latch region against the PAS core. Release of the latch, observed both experimentally and in the simulations, is known to mediate light-induced VVD dimerization. This computational study of a LOV protein, unprecedented in its agreement with experiment, provides an atomistic view of long-range allosteric coupling in a photoreceptor.

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Language(s): eng - English
 Dates: 2016-10-122017-02-012017-03-01
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jacs.6b10701
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Title: Journal of the American Chemical Society
  Other : J. Am. Chem. Soc.
  Abbreviation : JACS
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 139 (8) Sequence Number: - Start / End Page: 2972 - 2980 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870