1xfn

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|PDB= 1xfn |SIZE=350|CAPTION= <scene name='initialview01'>1xfn</scene>
|PDB= 1xfn |SIZE=350|CAPTION= <scene name='initialview01'>1xfn</scene>
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=HC4:4'-HYDROXYCINNAMIC ACID'>HC4</scene>
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|LIGAND= <scene name='pdbligand=HC4:4&#39;-HYDROXYCINNAMIC ACID'>HC4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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[[Category: pas domain]]
[[Category: pas domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:09:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:12:52 2008''

Revision as of 12:12, 23 March 2008


PDB ID 1xfn

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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. 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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