1s1y

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(New page: 200px<br /><applet load="1s1y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s1y, resolution 1.6&Aring;" /> '''Photoactivated chromo...)
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[[Image:1s1y.jpg|left|200px]]<br /><applet load="1s1y" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1s1y.jpg|left|200px]]<br /><applet load="1s1y" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1s1y, resolution 1.6&Aring;" />
caption="1s1y, resolution 1.6&Aring;" />
'''Photoactivated chromophore conformation in Photoactive Yellow Protein (E46Q mutant) from 10 microseconds to 3 milliseconds'''<br />
'''Photoactivated chromophore conformation in Photoactive Yellow Protein (E46Q mutant) from 10 microseconds to 3 milliseconds'''<br />
==Overview==
==Overview==
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We use time-resolved crystallography to observe the structural progression, of a bacterial blue light photoreceptor throughout its photocycle. Data, were collected from 10 ns to 100 ms after photoactivation of the E46Q, mutant of photoactive yellow protein. Refinement of transient chromophore, conformations shows that the spectroscopically distinct intermediates are, formed via progressive disruption of the hydrogen bond network to the, chromophore. Although structural change occurs within a few nanoseconds on, and around the chromophore, it takes milliseconds for a distinct pattern, of tertiary structural change to fully progress through the entire, molecule, thus generating the putative signaling state. Remarkably, the, coupling between the chromophore conformation and the tertiary structure, of this small protein is not tight: there are leads and lags between, changes in the conformation of the chromophore and the protein tertiary, structure.
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We use time-resolved crystallography to observe the structural progression of a bacterial blue light photoreceptor throughout its photocycle. Data were collected from 10 ns to 100 ms after photoactivation of the E46Q mutant of photoactive yellow protein. Refinement of transient chromophore conformations shows that the spectroscopically distinct intermediates are formed via progressive disruption of the hydrogen bond network to the chromophore. Although structural change occurs within a few nanoseconds on and around the chromophore, it takes milliseconds for a distinct pattern of tertiary structural change to fully progress through the entire molecule, thus generating the putative signaling state. Remarkably, the coupling between the chromophore conformation and the tertiary structure of this small protein is not tight: there are leads and lags between changes in the conformation of the chromophore and the protein tertiary structure.
==About this Structure==
==About this Structure==
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1S1Y 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=1S1Y OCA].
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1S1Y 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=1S1Y OCA].
==Reference==
==Reference==
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[[Category: time-resolved]]
[[Category: time-resolved]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:02:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:08 2008''

Revision as of 12:57, 21 February 2008


1s1y, resolution 1.6Å

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Photoactivated chromophore conformation in Photoactive Yellow Protein (E46Q mutant) from 10 microseconds to 3 milliseconds

Overview

We use time-resolved crystallography to observe the structural progression of a bacterial blue light photoreceptor throughout its photocycle. Data were collected from 10 ns to 100 ms after photoactivation of the E46Q mutant of photoactive yellow protein. Refinement of transient chromophore conformations shows that the spectroscopically distinct intermediates are formed via progressive disruption of the hydrogen bond network to the chromophore. Although structural change occurs within a few nanoseconds on and around the chromophore, it takes milliseconds for a distinct pattern of tertiary structural change to fully progress through the entire molecule, thus generating the putative signaling state. Remarkably, the coupling between the chromophore conformation and the tertiary structure of this small protein is not tight: there are leads and lags between changes in the conformation of the chromophore and the protein tertiary structure.

About this Structure

1S1Y is a Single protein structure of sequence from Halorhodospira halophila with as ligand. Full crystallographic information is available from OCA.

Reference

Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein., Anderson S, Srajer V, Pahl R, Rajagopal S, Schotte F, Anfinrud P, Wulff M, Moffat K, Structure. 2004 Jun;12(6):1039-45. PMID:15274923

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