Structure of a protein photocycle intermediate by millisecond time- resolved crystallography

Ulrich K. Genick, Gloria E.O. Borgstahl, Kingman Ng, Zhong Ren, Claude Pradervand, Patrick M. Burke, Vukica Šrajer, Tsu Yi Teng, Wilfried Schildkamp, Duncan E. McRee, Keith Moffat, Elizabeth D. Getzoff

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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.

Original languageEnglish (US)
Pages (from-to)1471-1475
Number of pages5
JournalScience
Volume275
Issue number5305
DOIs
StatePublished - Mar 7 1997

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Cite this

Genick, U. K., Borgstahl, G. E. O., Ng, K., Ren, Z., Pradervand, C., Burke, P. M., Šrajer, V., Teng, T. Y., Schildkamp, W., McRee, D. E., Moffat, K., & Getzoff, E. D. (1997). Structure of a protein photocycle intermediate by millisecond time- resolved crystallography. Science, 275(5305), 1471-1475. https://doi.org/10.1126/science.275.5305.1471