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Seminar

Resolving Paradoxes in Protein Photocycles at Atomic Resolution:Structural and Mutational Analyses of Photoactive Yellow Protein

Monday, April 19, 1999
3:00 pm
3269 Beckman Institute

To understand in atomic detail how a chromophore and a protein interact to sense light and send a biological signal, we are pursuing coupled mutational, biochemical, spectroscopic, computational, and structural studies of the bacterial blue-light photoreceptor photoactive yellow protein (PYP). The three high resolution crystallographic structures that we have determined for intermediates in the photocycle of PYP reveal the interplay between protein and chromophore that mediates the conversion of light energy into a biological signal. Additionally, we have identified PYP as the structural prototype for the three-dimensional fold of the PAS domain superfamily, which encompasses diverse proteins primarily involved in signal-transduction pathways in all three kingdoms of life.

Genick et al., 1997, ``Structure of a protein photocycle intermediate by millisecond time-resolved crystallography'', Science 275, 1471-1475.

Genick et al., 1998, ``Structure at 0.85 A resolution of an early protein photocycle intermediate'', Nature 392, 206-209.

Pellequer et al., 1998, ``Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain superfamily'', Proc. Natl. Acad. Sci. USA 95, 5884-5890.