1XFN

NMR structure of the ground state of the photoactive yellow protein lacking the N-terminal part

Summary for 1XFN

• Entry DOI: 10.2210/pdb1xfn/pdb
• Related: 1ODV 1XFQ 2phy
• NMR Information: BMRB: 6321
• Descriptor: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (2 entities in total)
• Functional Keywords: pas domain, signaling protein
• Biological source: Halorhodospira halophila
• Total number of polymer chains: 1
• Total formula weight: 12980.42

Authors

Bernard, C.,Houben, K.,Derix, N.M.,Marks, D.,van der Horst, M.A.,Hellingwerf, K.J.,Boelens, R.,Kaptein, R.,van Nuland, N.A. (deposition date: 2004-09-15, release date: 2005-08-16, Last modification date: 2022-03-02)

Primary citation

Bernard, C.,Houben, K.,Derix, N.M.,Marks, D.,van der Horst, M.A.,Hellingwerf, K.J.,Boelens, R.,Kaptein, R.,van Nuland, N.A.
The solution structure of a transient photoreceptor intermediate: delta25 photoactive yellow protein
STRUCTURE, 13:953-962, 2005

PubMed Abstract: 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.

PubMed: 16004868
DOI: 10.1016/j.str.2005.04.017

Experimental method

SOLUTION NMR