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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1xfn.gif|left|200px]]<br /><applet load="1xfn" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1xfn" />
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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==
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.
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==
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].  
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.]]
[[Category: Derix, N.M.]]
[[Category: Derix, N M.]]
[[Category: Hellingwerf, K.J.]]
[[Category: Hellingwerf, K J.]]
[[Category: Horst, M.A.van.der.]]
[[Category: Horst, M A.van der.]]
[[Category: Houben, K.]]
[[Category: Houben, K.]]
[[Category: Kaptein, R.]]
[[Category: Kaptein, R.]]
[[Category: Marks, D.]]
[[Category: Marks, D.]]
[[Category: Nuland, N.A.van.]]
[[Category: Nuland, N A.van.]]
[[Category: HC4]]
[[Category: HC4]]
[[Category: pas domain]]
[[Category: pas domain]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:02:49 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:16 2008''