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2PYR

PHOTOACTIVE YELLOW PROTEIN, 1 NANOSECOND INTERMEDIATE (287K)

Summary for 2PYR
Entry DOI10.2210/pdb2pyr/pdb
DescriptorPHOTOACTIVE YELLOW PROTEIN, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
Functional Keywordsphotoreceptor, light sensor for negative phototaxis
Biological sourceHalorhodospira halophila
Total number of polymer chains1
Total formula weight14052.73
Authors
Perman, B.,Srajer, V.,Ren, Z.,Teng, T.Y.,Pradervand, C.,Ursby, T.,Bourgeois, D.,Schotte, F.,Wulff, M.,Kort, R.,Hellingwerf, K.,Moffat, K. (deposition date: 1998-03-04, release date: 1999-04-06, Last modification date: 2011-07-13)
Primary citationPerman, B.,Srajer, V.,Ren, Z.,Teng, T.,Pradervand, C.,Ursby, T.,Bourgeois, D.,Schotte, F.,Wulff, M.,Kort, R.,Hellingwerf, K.,Moffat, K.
Energy transduction on the nanosecond time scale: early structural events in a xanthopsin photocycle.
Science, 279:1946-1950, 1998
Cited by
PubMed Abstract: Photoactive yellow protein (PYP) is a member of the xanthopsin family of eubacterial blue-light photoreceptors. On absorption of light, PYP enters a photocycle that ultimately transduces the energy contained in a light signal into an altered biological response. Nanosecond time-resolved x-ray crystallography was used to determine the structure of the short-lived, red-shifted, intermediate state denoted [pR], which develops within 1 nanosecond after photoelectronic excitation of the chromophore of PYP by absorption of light. The resulting structural model demonstrates that the [pR] state possesses the cis conformation of the 4-hydroxyl cinnamic thioester chromophore, and that the process of trans to cis isomerization is accompanied by the specific formation of new hydrogen bonds that replace those broken upon excitation of the chromophore. Regions of flexibility that compose the chromophore-binding pocket serve to lower the activation energy barrier between the dark state, denoted pG, and [pR], and help initiate entrance into the photocycle. Direct structural evidence is provided for the initial processes of transduction of light energy, which ultimately translate into a physiological signal.
PubMed: 9506946
DOI: 10.1126/science.279.5358.1946
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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