1uwp
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The light-induced isomerization of a double bond is the key event that | + | The light-induced isomerization of a double bond is the key event that allows the conversion of light energy into a structural change in photoactive proteins for many light-mediated biological processes, such as vision, photosynthesis, photomorphogenesis, and photo movement. Cofactors such as retinals, linear tetrapyrroles, and 4-hydroxy-cinnamic acid have been selected by nature that provide the essential double bond to transduce the light signal into a conformational change and eventually, a physiological response. Here we report the first events after light excitation of the latter chromophore, containing a single ethylene double bond, in a low temperature crystallographic study of the photoactive yellow protein. We measured experimental phases to overcome possible model bias, corrected for minimized radiation damage, and measured absorption spectra of crystals to analyze the photoproducts formed. The data show a mechanism for the light activation of photoactive yellow protein, where the energy to drive the remainder of the conformational changes is stored in a slightly strained but fully cis-chromophore configuration. In addition, our data indicate a role for backbone rearrangements during the very early structural events. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Halorhodospira halophila]] | [[Category: Halorhodospira halophila]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hellingwerf, K | + | [[Category: Hellingwerf, K J.]] |
[[Category: Kort, R.]] | [[Category: Kort, R.]] | ||
| - | [[Category: Ravelli, R | + | [[Category: Ravelli, R B.G.]] |
[[Category: HC4]] | [[Category: HC4]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: yellow]] | [[Category: yellow]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:29:05 2008'' |
Revision as of 13:29, 21 February 2008
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INITIAL EVENTS IN THE PHOTOCYCLE OF PHOTOACTIVE YELLOW PROTEIN
Overview
The light-induced isomerization of a double bond is the key event that allows the conversion of light energy into a structural change in photoactive proteins for many light-mediated biological processes, such as vision, photosynthesis, photomorphogenesis, and photo movement. Cofactors such as retinals, linear tetrapyrroles, and 4-hydroxy-cinnamic acid have been selected by nature that provide the essential double bond to transduce the light signal into a conformational change and eventually, a physiological response. Here we report the first events after light excitation of the latter chromophore, containing a single ethylene double bond, in a low temperature crystallographic study of the photoactive yellow protein. We measured experimental phases to overcome possible model bias, corrected for minimized radiation damage, and measured absorption spectra of crystals to analyze the photoproducts formed. The data show a mechanism for the light activation of photoactive yellow protein, where the energy to drive the remainder of the conformational changes is stored in a slightly strained but fully cis-chromophore configuration. In addition, our data indicate a role for backbone rearrangements during the very early structural events.
About this Structure
1UWP is a Single protein structure of sequence from Halorhodospira halophila with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Initial events in the photocycle of photoactive yellow protein., Kort R, Hellingwerf KJ, Ravelli RB, J Biol Chem. 2004 Jun 18;279(25):26417-24. Epub 2004 Mar 16. PMID:15026418
Page seeded by OCA on Thu Feb 21 15:29:05 2008
Categories: Halorhodospira halophila | Single protein | Hellingwerf, K J. | Kort, R. | Ravelli, R B.G. | HC4 | SO4 | Domains | Fold photocycle | Gaf | Lov | Pas | Photoactive | Photoreceptor | Signaling protein | Yellow
