Structural highlights
Function
[PYP_HALHA] Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In the bacterial photoreceptor photoactive yellow protein (PYP), absorption of blue light by its chromophore leads to a conformational change in the protein associated with differential signaling activity, as it executes a reversible photocycle. Time-resolved Laue crystallography allows structural snapshots (as short as 150 ps) of high crystallographic resolution (approximately 1.6 A) to be taken of a protein as it functions. Here, we analyze by singular value decomposition a comprehensive time-resolved crystallographic data set of the E46Q mutant of PYP throughout the photocycle spanning 10 ns-100 ms. We identify and refine the structures of five distinct intermediates and provide a plausible chemical kinetic mechanism for their inter conversion. A clear structural progression is visible in these intermediates, in which a signal generated at the chromophore propagates through a distinct structural pathway of conserved residues and results in structural changes near the N terminus, over 20 A distant from the chromophore.
A structural pathway for signaling in the E46Q mutant of photoactive yellow protein.,Rajagopal S, Anderson S, Srajer V, Schmidt M, Pahl R, Moffat K Structure. 2005 Jan;13(1):55-63. PMID:15642261[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rajagopal S, Anderson S, Srajer V, Schmidt M, Pahl R, Moffat K. A structural pathway for signaling in the E46Q mutant of photoactive yellow protein. Structure. 2005 Jan;13(1):55-63. PMID:15642261 doi:10.1016/j.str.2004.10.016
