1t1c
From Proteopedia
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Late intermediate IL3 from time-resolved crystallography of the E46Q mutant of PYP
Overview
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.
About this Structure
1T1C is a Single protein structure of sequence from Halorhodospira halophila with HC4 as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 02:55:06 2007
