1t1c

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(New page: 200px<br /><applet load="1t1c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t1c, resolution 1.60&Aring;" /> '''Late intermediate IL...)
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[[Image:1t1c.gif|left|200px]]<br /><applet load="1t1c" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1t1c.gif|left|200px]]<br /><applet load="1t1c" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1t1c, resolution 1.60&Aring;" />
caption="1t1c, resolution 1.60&Aring;" />
'''Late intermediate IL3 from time-resolved crystallography of the E46Q mutant of PYP'''<br />
'''Late intermediate IL3 from time-resolved crystallography of the E46Q mutant of PYP'''<br />
==Overview==
==Overview==
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In the bacterial photoreceptor photoactive yellow protein (PYP), absorption of blue light by its chromophore leads to a conformational, change in the protein associated with differential signaling activity, as, it executes a reversible photocycle. Time-resolved Laue crystallography, allows structural snapshots (as short as 150 ps) of high crystallographic, resolution (approximately 1.6 A) to be taken of a protein as it functions., Here, we analyze by singular value decomposition a comprehensive, time-resolved crystallographic data set of the E46Q mutant of PYP, throughout the photocycle spanning 10 ns-100 ms. We identify and refine, the structures of five distinct intermediates and provide a plausible, chemical kinetic mechanism for their inter conversion. A clear structural, progression is visible in these intermediates, in which a signal generated, at the chromophore propagates through a distinct structural pathway of, conserved residues and results in structural changes near the N terminus, over 20 A distant from the chromophore.
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In the bacterial photoreceptor photoactive yellow protein (PYP), absorption of blue light by its chromophore leads to a conformational change in the protein associated with differential signaling activity, as it executes a reversible photocycle. Time-resolved Laue crystallography allows structural snapshots (as short as 150 ps) of high crystallographic resolution (approximately 1.6 A) to be taken of a protein as it functions. Here, we analyze by singular value decomposition a comprehensive time-resolved crystallographic data set of the E46Q mutant of PYP throughout the photocycle spanning 10 ns-100 ms. We identify and refine the structures of five distinct intermediates and provide a plausible chemical kinetic mechanism for their inter conversion. A clear structural progression is visible in these intermediates, in which a signal generated at the chromophore propagates through a distinct structural pathway of conserved residues and results in structural changes near the N terminus, over 20 A distant from the chromophore.
==About this Structure==
==About this Structure==
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1T1C 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=1T1C OCA].
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1T1C 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=1T1C OCA].
==Reference==
==Reference==
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[[Category: photoactive yellow protein]]
[[Category: photoactive yellow protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:55:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:51 2008''

Revision as of 13:08, 21 February 2008


1t1c, resolution 1.60Å

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Late intermediate IL3 from time-resolved crystallography of the E46Q mutant of PYP

Overview

In the bacterial photoreceptor photoactive yellow protein (PYP), absorption of blue light by its chromophore leads to a conformational change in the protein associated with differential signaling activity, as it executes a reversible photocycle. Time-resolved Laue crystallography allows structural snapshots (as short as 150 ps) of high crystallographic resolution (approximately 1.6 A) to be taken of a protein as it functions. Here, we analyze by singular value decomposition a comprehensive time-resolved crystallographic data set of the E46Q mutant of PYP throughout the photocycle spanning 10 ns-100 ms. We identify and refine the structures of five distinct intermediates and provide a plausible chemical kinetic mechanism for their inter conversion. A clear structural progression is visible in these intermediates, in which a signal generated at the chromophore propagates through a distinct structural pathway of conserved residues and results in structural changes near the N terminus, over 20 A distant from the chromophore.

About this Structure

1T1C is a Single protein structure of sequence from Halorhodospira halophila with as ligand. Full crystallographic information is available from OCA.

Reference

A structural pathway for signaling in the E46Q mutant of photoactive yellow protein., Rajagopal S, Anderson S, Srajer V, Schmidt M, Pahl R, Moffat K, Structure. 2005 Jan;13(1):55-63. PMID:15642261

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