1lls
From Proteopedia
(New page: 200px<br /><applet load="1lls" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lls, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1lls.jpg|left|200px]]<br /><applet load="1lls" size=" | + | [[Image:1lls.jpg|left|200px]]<br /><applet load="1lls" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lls, resolution 1.80Å" /> | caption="1lls, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE OF UNLIGANDED MALTOSE BINDING PROTEIN WITH XENON'''<br /> | '''CRYSTAL STRUCTURE OF UNLIGANDED MALTOSE BINDING PROTEIN WITH XENON'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Xenon-binding sites in proteins have led to a number of applications of | + | Xenon-binding sites in proteins have led to a number of applications of xenon in biochemical and structural studies. Here we further develop the utility of 129Xe NMR in characterizing specific xenon-protein interactions. The sensitivity of the 129Xe chemical shift to its local environment and the intense signals attainable by optical pumping make xenon a useful NMR reporter of its own interactions with proteins. A method for detecting specific xenon-binding interactions by analysis of 129Xe chemical shift data is illustrated using the maltose binding protein (MBP) from Escherichia coli as an example. The crystal structure of MBP in the presence of 8atm of xenon confirms the binding site determined from NMR data. Changes in the structure of the xenon-binding cavity upon the binding of maltose by the protein can account for the sensitivity of the 129Xe chemical shift to MBP conformation. 129Xe NMR data for xenon in solution with a number of cavity containing phage T4 lysozyme mutants show that xenon can report on cavity structure. In particular, a correlation exists between cavity size and the binding-induced 129Xe chemical shift. Further applications of 129Xe NMR to biochemical assays, including the screening of proteins for xenon binding for crystallography are considered. |
==About this Structure== | ==About this Structure== | ||
| - | 1LLS 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 XE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LLS 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=XE:'>XE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lee, S | + | [[Category: Lee, S Y.]] |
[[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: XE]] | [[Category: XE]] | ||
[[Category: hydrophobic cavities]] | [[Category: hydrophobic cavities]] | ||
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[[Category: xenon derivative]] | [[Category: xenon derivative]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:09 2008'' |
Revision as of 11:46, 21 February 2008
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CRYSTAL STRUCTURE OF UNLIGANDED MALTOSE BINDING PROTEIN WITH XENON
Overview
Xenon-binding sites in proteins have led to a number of applications of xenon in biochemical and structural studies. Here we further develop the utility of 129Xe NMR in characterizing specific xenon-protein interactions. The sensitivity of the 129Xe chemical shift to its local environment and the intense signals attainable by optical pumping make xenon a useful NMR reporter of its own interactions with proteins. A method for detecting specific xenon-binding interactions by analysis of 129Xe chemical shift data is illustrated using the maltose binding protein (MBP) from Escherichia coli as an example. The crystal structure of MBP in the presence of 8atm of xenon confirms the binding site determined from NMR data. Changes in the structure of the xenon-binding cavity upon the binding of maltose by the protein can account for the sensitivity of the 129Xe chemical shift to MBP conformation. 129Xe NMR data for xenon in solution with a number of cavity containing phage T4 lysozyme mutants show that xenon can report on cavity structure. In particular, a correlation exists between cavity size and the binding-induced 129Xe chemical shift. Further applications of 129Xe NMR to biochemical assays, including the screening of proteins for xenon binding for crystallography are considered.
About this Structure
1LLS is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy., Rubin SM, Lee SY, Ruiz EJ, Pines A, Wemmer DE, J Mol Biol. 2002 Sep 13;322(2):425-40. PMID:12217701
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