1T19

Early intermediate IE2 from time-resolved crystallography of the E46Q mutant of PYP

Summary for 1T19

• Entry DOI: 10.2210/pdb1t19/pdb
• Related: 1T18 1T1A 1T1B 1T1C
• Descriptor: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (2 entities in total)
• Functional Keywords: photoactive yellow protein, pas domain, photoreceptor
• Biological source: Halorhodospira halophila
• Total number of polymer chains: 1
• Total formula weight: 14051.75

Authors

Rajagopal, S.,Anderson, S.,Srajer, V.,Schmidt, M.,Pahl, R.,Moffat, K. (deposition date: 2004-04-15, release date: 2005-01-18, Last modification date: 2021-10-27)

Primary citation

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, 13:55-63, 2005

PubMed Abstract: 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.

PubMed: 15642261
DOI: 10.1016/j.str.2004.10.016

Experimental method

X-RAY DIFFRACTION (1.6 Å)