1xfn
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(New page: 200px<br /><applet load="1xfn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xfn" /> '''NMR structure of the ground state of the pho...)
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Revision as of 03:55, 21 November 2007
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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 with HC4 as ligand. 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
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