1UWP

Initial Events in the Photocycle of Photoactive Yellow Protein

Summary for 1UWP

• Entry DOI: 10.2210/pdb1uwp/pdb
• Related: 1D7E 1F98 1F9I 1GSV 1GSW 1GSX 1KOU 1NWZ 1ODV 1UWN 2PHY 2PYP 2PYR 3PHY 3PYP
• Descriptor: PHOTOACTIVE YELLOW PROTEIN, 4'-HYDROXYCINNAMIC ACID, SULFATE ION, ... (4 entities in total)
• Functional Keywords: signaling protein, pas, lov, gaf, domains, fold photocycle, photoactive, photoreceptor, yellow
• Biological source: HALORHODOSPIRA HALOPHILA
• Total number of polymer chains: 1
• Total formula weight: 14479.34

Authors

Kort, R.,Hellingwerf, K.J.,Ravelli, R.B.G. (deposition date: 2004-02-11, release date: 2006-05-10, Last modification date: 2025-04-09)

Primary citation

Kort, R.,Hellingwerf, K.J.,Ravelli, R.B.
Initial events in the photocycle of photoactive yellow protein.
J. Biol. Chem., 279:26417-26424, 2004

PubMed Abstract: 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.

PubMed: 15026418
DOI: 10.1074/jbc.M311961200

Experimental method

X-RAY DIFFRACTION (1.2 Å)