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New page: left|200px<br /><applet load="2bn8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bn8" /> '''SOLUTION STRUCTURE AND INTERACTIONS OF THE E...
 
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[[Image:2bn8.jpg|left|200px]]<br /><applet load="2bn8" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2bn8.jpg|left|200px]]<br /><applet load="2bn8" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2bn8" />
caption="2bn8" />
'''SOLUTION STRUCTURE AND INTERACTIONS OF THE E.COLI CELL DIVISION ACTIVATOR PROTEIN CEDA'''<br />
'''SOLUTION STRUCTURE AND INTERACTIONS OF THE E.COLI CELL DIVISION ACTIVATOR PROTEIN CEDA'''<br />


==Overview==
==Overview==
CedA is a protein that is postulated to be involved in the regulation of, cell division in Escherichia coli and related organisms; however, little, biological data about its possible mode of action are available. Here we, present a three-dimensional structure of this protein as determined by NMR, spectroscopy. The protein is made up of four antiparallel beta-strands, an, alpha-helix, and a large unstructured stretch of residues at the, N-terminus. It shows structural similarity to a family of DNA-binding, proteins which interact with dsDNA via a three-stranded beta-sheet, suggesting that CedA may be a DNA-binding protein. The putative binding, surface of CedA is predominantly positively charged with a number of basic, residues surrounding a groove largely dominated by aromatic residues. NMR, chemical shift perturbations and gel-shift experiments performed with CedA, confirm that the protein binds dsDNA, and its interaction is mediated, primarily via the beta-sheet.
CedA is a protein that is postulated to be involved in the regulation of cell division in Escherichia coli and related organisms; however, little biological data about its possible mode of action are available. Here we present a three-dimensional structure of this protein as determined by NMR spectroscopy. The protein is made up of four antiparallel beta-strands, an alpha-helix, and a large unstructured stretch of residues at the N-terminus. It shows structural similarity to a family of DNA-binding proteins which interact with dsDNA via a three-stranded beta-sheet, suggesting that CedA may be a DNA-binding protein. The putative binding surface of CedA is predominantly positively charged with a number of basic residues surrounding a groove largely dominated by aromatic residues. NMR chemical shift perturbations and gel-shift experiments performed with CedA confirm that the protein binds dsDNA, and its interaction is mediated primarily via the beta-sheet.


==About this Structure==
==About this Structure==
2BN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BN8 OCA].  
2BN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BN8 OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chen, H.A.]]
[[Category: Chen, H A.]]
[[Category: Huyton, T.]]
[[Category: Huyton, T.]]
[[Category: Matthews, S.]]
[[Category: Matthews, S.]]
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[[Category: cell division activator protein]]
[[Category: cell division activator protein]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:37 2008''