2QJ5

PYP ultra-high resolution of a bacterial photoreceptor

Summary for 2QJ5

• Entry DOI: 10.2210/pdb2qj5/pdb
• Related: 2QJ7
• Descriptor: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• Functional Keywords: pas domain, signaling protein
• Biological source: Halorhodospira halophila
• Total number of polymer chains: 1
• Total formula weight: 14052.73

Authors

Coureux, P.D.,Fan, Z.P.,Stojanoff, V.,Genick, U.K. (deposition date: 2007-07-06, release date: 2008-05-20, Last modification date: 2023-08-30)

Primary citation

Coureux, P.D.,Fan, Z.P.,Stojanoff, V.,Genick, U.K.
Picometer-scale conformational heterogeneity separates functional from nonfunctional States of a photoreceptor protein.
Structure, 16:863-872, 2008

PubMed Abstract: Protein structural fluctuations occur over a wide spatial scale, ranging from minute, picometer-scale displacements, to large, interdomain motions and partial unfolding. While large-scale protein structural changes and their effects on protein function have been the focus of much recent attention, small-scale fluctuations have been less well studied, and are generally assumed to have proportionally smaller effects. Here we use the bacterial photoreceptor photoactive yellow protein (PYP) to test if subtle structural changes do, indeed, imply equally subtle functional effects. We flash froze crystals of PYP to trap the protein's conformational ensemble, and probed the molecules in this ensemble for their ability to facilitate PYP's biological function (i.e., light-driven isomerization of its chromophore). Our results indicate that the apparently homogeneous structural state observed in a 0.82 A crystal structure in fact comprises an ensemble of conformational states, in which subpopulations with nearly identical structures display dramatically different functional properties.

PubMed: 18547519
DOI: 10.1016/j.str.2008.02.022

Experimental method

X-RAY DIFFRACTION (1.2 Å)