2PYP

PHOTOACTIVE YELLOW PROTEIN, PHOTOSTATIONARY STATE, 50% GROUND STATE, 50% BLEACHED

Summary for 2PYP

• Entry DOI: 10.2210/pdb2pyp/pdb
• Descriptor: Photoactive yellow protein (2 entities in total)
• Functional Keywords: photoreceptor, chromophore, light sensor for phototaxis
• Biological source: Halorhodospira halophila
• Total number of polymer chains: 1
• Total formula weight: 14034.72

Authors

Genick, U.K.,Borgstahl, G.E.O.,Ng, K.,Ren, Z.,Pradervand, C.,Burke, P.,Srajer, V.,Teng, T.,Schildkamp, W.,Mcree, D.E.,Moffat, K.,Getzoff, E.D. (deposition date: 1997-02-03, release date: 1998-04-29, Last modification date: 2024-12-25)

Primary citation

Genick, U.K.,Borgstahl, G.E.,Ng, K.,Ren, Z.,Pradervand, C.,Burke, P.M.,Srajer, V.,Teng, T.Y.,Schildkamp, W.,McRee, D.E.,Moffat, K.,Getzoff, E.D.
Structure of a protein photocycle intermediate by millisecond time-resolved crystallography.
Science, 275:1471-1475, 1997

PubMed Abstract: The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a self-contained light cycle. The atomic structure of the bleached signaling intermediate in the light cycle of PYP was determined by millisecond time-resolved, multiwavelength Laue crystallography and simultaneous optical spectroscopy. Light-induced trans-to-cis isomerization of the 4-hydroxycinnamyl chromophore and coupled protein rearrangements produce a new set of active-site hydrogen bonds. An arginine gateway opens, allowing solvent exposure and protonation of the chromophore's phenolic oxygen. Resulting changes in shape, hydrogen bonding, and electrostatic potential at the protein surface form a likely basis for signal transduction. The structural results suggest a general framework for the interpretation of protein photocycles.

PubMed: 9045611
DOI: 10.1126/science.275.5305.1471

Experimental method

X-RAY DIFFRACTION (1.9 Å)