1nwz

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(New page: 200px<br /><applet load="1nwz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nwz, resolution 0.82&Aring;" /> '''PYP ULTRA-HIGH RESOL...)
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[[Image:1nwz.gif|left|200px]]<br /><applet load="1nwz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nwz, resolution 0.82&Aring;" />
caption="1nwz, resolution 0.82&Aring;" />
'''PYP ULTRA-HIGH RESOLUTION STRUCTURE OF A BACTERIAL PHOTORECEPTOR'''<br />
'''PYP ULTRA-HIGH RESOLUTION STRUCTURE OF A BACTERIAL PHOTORECEPTOR'''<br />
==Overview==
==Overview==
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Protein photoreceptors use small-molecule cofactors called chromophores to, detect light. Only under the influence of the receptors' active sites do, these chromophores adopt spectral and photochemical properties that suit, the receptors' functional requirements. This protein-induced change in, chromophore properties is called photochemical tuning and is a prime, example for the general--but poorly understood--process of chemical tuning, through which proteins shape the reactivity of their active-site groups., Here we report the 0.82-A resolution X-ray structure of the bacterial, light receptor photoactive yellow protein (PYP). The unusually precise, structure reveals deviations from expected molecular geometries and, anisotropic atomic displacements in the PYP active site. Our analysis of, these deviations points directly to the intramolecular forces and, active-site dynamics that tune the properties of PYP's chromophore to, absorb blue light, suppress fluorescence, and favor the required, light-driven double-bond isomerization.
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Protein photoreceptors use small-molecule cofactors called chromophores to detect light. Only under the influence of the receptors' active sites do these chromophores adopt spectral and photochemical properties that suit the receptors' functional requirements. This protein-induced change in chromophore properties is called photochemical tuning and is a prime example for the general--but poorly understood--process of chemical tuning through which proteins shape the reactivity of their active-site groups. Here we report the 0.82-A resolution X-ray structure of the bacterial light receptor photoactive yellow protein (PYP). The unusually precise structure reveals deviations from expected molecular geometries and anisotropic atomic displacements in the PYP active site. Our analysis of these deviations points directly to the intramolecular forces and active-site dynamics that tune the properties of PYP's chromophore to absorb blue light, suppress fluorescence, and favor the required light-driven double-bond isomerization.
==About this Structure==
==About this Structure==
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1NWZ 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=1NWZ OCA].
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1NWZ 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=1NWZ OCA].
==Reference==
==Reference==
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[[Category: Halorhodospira halophila]]
[[Category: Halorhodospira halophila]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Genick, U.K.]]
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[[Category: Genick, U K.]]
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[[Category: Getzoff, E.D.]]
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[[Category: Getzoff, E D.]]
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[[Category: Gutwin, K.N.]]
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[[Category: Gutwin, K N.]]
[[Category: HC4]]
[[Category: HC4]]
[[Category: domains fold]]
[[Category: domains fold]]
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[[Category: pas]]
[[Category: pas]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:37:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:58 2008''

Revision as of 12:10, 21 February 2008

Image:1nwz.gif

1nwz, resolution 0.82Å

Drag the structure with the mouse to rotate

PYP ULTRA-HIGH RESOLUTION STRUCTURE OF A BACTERIAL PHOTORECEPTOR

Overview

Protein photoreceptors use small-molecule cofactors called chromophores to detect light. Only under the influence of the receptors' active sites do these chromophores adopt spectral and photochemical properties that suit the receptors' functional requirements. This protein-induced change in chromophore properties is called photochemical tuning and is a prime example for the general--but poorly understood--process of chemical tuning through which proteins shape the reactivity of their active-site groups. Here we report the 0.82-A resolution X-ray structure of the bacterial light receptor photoactive yellow protein (PYP). The unusually precise structure reveals deviations from expected molecular geometries and anisotropic atomic displacements in the PYP active site. Our analysis of these deviations points directly to the intramolecular forces and active-site dynamics that tune the properties of PYP's chromophore to absorb blue light, suppress fluorescence, and favor the required light-driven double-bond isomerization.

About this Structure

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

Reference

Anticipatory active-site motions and chromophore distortion prime photoreceptor PYP for light activation., Getzoff ED, Gutwin KN, Genick UK, Nat Struct Biol. 2003 Aug;10(8):663-8. PMID:12872160

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