2pyp: Difference between revisions

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New page: left|200px<br /><applet load="2pyp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pyp, resolution 1.9Å" /> '''PHOTOACTIVE YELLOW PR...
 
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[[Image:2pyp.jpg|left|200px]]<br /><applet load="2pyp" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2pyp.jpg|left|200px]]<br /><applet load="2pyp" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2pyp, resolution 1.9&Aring;" />
caption="2pyp, resolution 1.9&Aring;" />
'''PHOTOACTIVE YELLOW PROTEIN, PHOTOSTATIONARY STATE, 50% GROUND STATE, 50% BLEACHED'''<br />
'''PHOTOACTIVE YELLOW PROTEIN, PHOTOSTATIONARY STATE, 50% GROUND STATE, 50% BLEACHED'''<br />


==Overview==
==Overview==
The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a, self-contained light cycle. The atomic structure of the bleached signaling, intermediate in the light cycle of PYP was determined by millisecond, time-resolved, multiwavelength Laue crystallography and simultaneous, optical spectroscopy. Light-induced trans-to-cis isomerization of the, 4-hydroxycinnamyl chromophore and coupled protein rearrangements produce a, new set of active-site hydrogen bonds. An arginine gateway opens, allowing, solvent exposure and protonation of the chromophore's phenolic oxygen., Resulting changes in shape, hydrogen bonding, and electrostatic potential, at the protein surface form a likely basis for signal transduction. The, structural results suggest a general framework for the interpretation of, protein photocycles.
The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a self-contained light cycle. The atomic structure of the bleached signaling intermediate in the light cycle of PYP was determined by millisecond time-resolved, multiwavelength Laue crystallography and simultaneous optical spectroscopy. Light-induced trans-to-cis isomerization of the 4-hydroxycinnamyl chromophore and coupled protein rearrangements produce a new set of active-site hydrogen bonds. An arginine gateway opens, allowing solvent exposure and protonation of the chromophore's phenolic oxygen. Resulting changes in shape, hydrogen bonding, and electrostatic potential at the protein surface form a likely basis for signal transduction. The structural results suggest a general framework for the interpretation of protein photocycles.


==About this Structure==
==About this Structure==
2PYP 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=2PYP OCA].  
2PYP 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=2PYP OCA].  


==Reference==
==Reference==
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[[Category: Halorhodospira halophila]]
[[Category: Halorhodospira halophila]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Borgstahl, G.E.O.]]
[[Category: Borgstahl, G E.O.]]
[[Category: Burke, P.]]
[[Category: Burke, P.]]
[[Category: Genick, U.K.]]
[[Category: Genick, U K.]]
[[Category: Getzoff, E.D.]]
[[Category: Getzoff, E D.]]
[[Category: Mcree, D.E.]]
[[Category: Mcree, D E.]]
[[Category: Moffat, K.]]
[[Category: Moffat, K.]]
[[Category: Ng, K.]]
[[Category: Ng, K.]]
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[[Category: photoreceptor]]
[[Category: photoreceptor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:44:17 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:34:17 2008''

Revision as of 19:34, 21 February 2008

File:2pyp.jpg


2pyp, resolution 1.9Å

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PHOTOACTIVE YELLOW PROTEIN, PHOTOSTATIONARY STATE, 50% GROUND STATE, 50% BLEACHED

OverviewOverview

The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a self-contained light cycle. The atomic structure of the bleached signaling intermediate in the light cycle of PYP was determined by millisecond time-resolved, multiwavelength Laue crystallography and simultaneous optical spectroscopy. Light-induced trans-to-cis isomerization of the 4-hydroxycinnamyl chromophore and coupled protein rearrangements produce a new set of active-site hydrogen bonds. An arginine gateway opens, allowing solvent exposure and protonation of the chromophore's phenolic oxygen. Resulting changes in shape, hydrogen bonding, and electrostatic potential at the protein surface form a likely basis for signal transduction. The structural results suggest a general framework for the interpretation of protein photocycles.

About this StructureAbout this Structure

2PYP is a Single protein structure of sequence from Halorhodospira halophila with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a protein photocycle intermediate by millisecond time-resolved crystallography., Genick UK, Borgstahl GE, Ng K, Ren Z, Pradervand C, Burke PM, Srajer V, Teng TY, Schildkamp W, McRee DE, Moffat K, Getzoff ED, Science. 1997 Mar 7;275(5305):1471-5. PMID:9045611

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