PH dependence of the photoactive yellow protein photocycle investigated by time-resolved crystallography.

ABSTRACT: Visualizing the three-dimensional structures of a protein during its biological activity is key to understanding its mechanism. In general, protein structure and function are pH-dependent. Changing the pH provides new insights into the mechanisms that are involved in protein activity. Photoactive yellow protein (PYP) is a signaling protein that serves as an ideal model for time-dependent studies on light-activated proteins. Its photocycle is studied extensively under different pH conditions. However, the structures of the intermediates remain unknown until time-resolved crystallography is employed. With the newest beamline developments, a comprehensive time series of Laue data can now be collected from a single protein crystal. This allows us to vary the pH. Here we present the first struc

SUBMITTER: Tripathi S 

PROVIDER: S-EPMC3260688 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature