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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[[Image:1xfn.gif|left|200px]]<br /><applet load="1xfn" size="350" color="white" frame="true" align="right" spinBox="true"
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'''NMR structure of the ground state of the photoactive yellow protein lacking the N-terminal part'''<br />
'''NMR structure of the ground state of the photoactive yellow protein lacking the N-terminal part'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1XFN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila] with HC4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XFN OCA].
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1XFN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila] with <scene name='pdbligand=HC4:'>HC4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFN OCA].
==Reference==
==Reference==
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[[Category: Bernard, C.]]
[[Category: Bernard, C.]]
[[Category: Boelens, R.]]
[[Category: Boelens, R.]]
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[[Category: Derix, N.M.]]
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[[Category: Derix, N M.]]
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[[Category: Hellingwerf, K.J.]]
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[[Category: Hellingwerf, K J.]]
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[[Category: Horst, M.A.van.der.]]
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[[Category: Horst, M A.van der.]]
[[Category: Houben, K.]]
[[Category: Houben, K.]]
[[Category: Kaptein, R.]]
[[Category: Kaptein, R.]]
[[Category: Marks, D.]]
[[Category: Marks, D.]]
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[[Category: Nuland, N.A.van.]]
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[[Category: Nuland, N A.van.]]
[[Category: HC4]]
[[Category: HC4]]
[[Category: pas domain]]
[[Category: pas domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:02:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:16 2008''

Revision as of 13:54, 21 February 2008


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 with 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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