1zdm
From Proteopedia
(New page: 200px<br /><applet load="1zdm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zdm, resolution 2.4Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1zdm.gif|left|200px]]<br /><applet load="1zdm" size=" | + | [[Image:1zdm.gif|left|200px]]<br /><applet load="1zdm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zdm, resolution 2.4Å" /> | caption="1zdm, resolution 2.4Å" /> | ||
'''Crystal Structure of Activated CheY Bound to Xe'''<br /> | '''Crystal Structure of Activated CheY Bound to Xe'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The chemical shift of the (129)Xe NMR signal has been shown to be | + | The chemical shift of the (129)Xe NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins. Here we show that the (129)Xe shift can sense more subtle changes: magnesium binding, BeF(3)(-) activation, and peptide binding by the Escherichia coli chemotaxis Y protein. (1)H-(15)N correlation spectroscopy and X-ray crystallography were used to identify two xenon-binding cavities in CheY that are primarily responsible for the shift changes. One site is near the active site, and the other is near the peptide binding site. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZDM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN and XE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1ZDM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=XE:'>XE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZDM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Doucleff, M.]] | [[Category: Doucleff, M.]] | ||
| - | [[Category: Lowery, T | + | [[Category: Lowery, T J.]] |
[[Category: Pines, A.]] | [[Category: Pines, A.]] | ||
| - | [[Category: Rubin, S | + | [[Category: Rubin, S M.]] |
| - | [[Category: Ruiz, E | + | [[Category: Ruiz, E J.]] |
| - | [[Category: Wemmer, D | + | [[Category: Wemmer, D E.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: XE]] | [[Category: XE]] | ||
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[[Category: xenon binding]] | [[Category: xenon binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:31 2008'' |
Revision as of 14:14, 21 February 2008
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Crystal Structure of Activated CheY Bound to Xe
Overview
The chemical shift of the (129)Xe NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins. Here we show that the (129)Xe shift can sense more subtle changes: magnesium binding, BeF(3)(-) activation, and peptide binding by the Escherichia coli chemotaxis Y protein. (1)H-(15)N correlation spectroscopy and X-ray crystallography were used to identify two xenon-binding cavities in CheY that are primarily responsible for the shift changes. One site is near the active site, and the other is near the peptide binding site.
About this Structure
1ZDM is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR., Lowery TJ, Doucleff M, Ruiz EJ, Rubin SM, Pines A, Wemmer DE, Protein Sci. 2005 Apr;14(4):848-55. Epub 2005 Mar 1. PMID:15741343
Page seeded by OCA on Thu Feb 21 16:14:31 2008
