2qj7
From Proteopedia
PYP ultra-high resolution of a bacterial photoreceptor
Structural highlights
FunctionPYP_HALHA Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response. Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein 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. Picometer-scale conformational heterogeneity separates functional from nonfunctional states of a photoreceptor protein.,Coureux PD, Fan ZP, Stojanoff V, Genick UK Structure. 2008 Jun;16(6):863-72. PMID:18547519[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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