1xfn
From Proteopedia
NMR structure of the ground state of the photoactive yellow protein lacking the N-terminal part
Overview
The N-terminally truncated variant of photoactive yellow protein (Delta25-PYP) undergoes a very similar photocycle as the corresponding wild-type protein (WT-PYP), although the lifetime of its light-illuminated (pB) state is much longer. This has allowed determination of the structure of both its dark- (pG) as well as its pB-state in solution by nuclear magnetic resonance (NMR) spectroscopy. The pG structure shows a well-defined fold, similar to WT-PYP and the X-ray structure of the pG state of Delta25-PYP. In the long-lived photocycle intermediate pB, the central beta sheet is still intact, as well as a small part of one alpha helix. The remainder of pB is unfolded and highly flexible, as evidenced by results from proton-deuterium exchange and NMR relaxation studies. Thus, the partially unfolded nature of the presumed signaling state of PYP in solution, as suggested previously, has now been structurally demonstrated.
About this Structure
1XFN is a Single protein structure of sequence from Halorhodospira halophila. Full crystallographic information is available from OCA.
Reference
The solution structure of a transient photoreceptor intermediate: Delta25 photoactive yellow protein., Bernard C, Houben K, Derix NM, Marks D, van der Horst MA, Hellingwerf KJ, Boelens R, Kaptein R, van Nuland NA, Structure. 2005 Jul;13(7):953-62. PMID:16004868 Page seeded by OCA on Sat May 3 14:58:03 2008
