2bn8: Difference between revisions

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[[~~Image~~:2bn8.~~png|left|200px~~]]

==SOLUTION STRUCTURE AND INTERACTIONS OF THE E.COLI CELL DIVISION ACTIVATOR PROTEIN CEDA==

== Structural highlights ==

<table><tr><td colspan='2'>[[2bn8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BN8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BN8 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bn8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bn8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bn8 PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

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.

~~{{STRUCTURE_2bn8| PDB=2bn8 | SCENE= }}~~

Solution structure and interactions of the Escherichia coli cell division activator protein CedA.,Chen HA, Simpson P, Huyton T, Roper D, Matthews S Biochemistry. 2005 May 10;44(18):6738-44. PMID:15865419<ref>PMID:15865419</ref>

~~===SOLUTION STRUCTURE AND INTERACTIONS OF THE E~~.~~COLI CELL DIVISION ACTIVATOR PROTEIN CEDA===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_15865419}}~~

== References ==

==~~About this Structure~~==

__TOC__

~~[[2bn8]] is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BN8 OCA].~~

</StructureSection>

[[Category: Escherichia coli]]

[[Category: Chen, H A.]]

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-[[Image:2bn8.png|left|200px]]
+==SOLUTION STRUCTURE AND INTERACTIONS OF THE E.COLI CELL DIVISION ACTIVATOR PROTEIN CEDA==
+<StructureSection load='2bn8' size='340' side='right' caption='[[2bn8]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2bn8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BN8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BN8 FirstGlance]. <br>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bn8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bn8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bn8 PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-{{STRUCTURE_2bn8|  PDB=2bn8  |  SCENE=  }}
+Solution structure and interactions of the Escherichia coli cell division activator protein CedA.,Chen HA, Simpson P, Huyton T, Roper D, Matthews S Biochemistry. 2005 May 10;44(18):6738-44. PMID:15865419<ref>PMID:15865419</ref>
-===SOLUTION STRUCTURE AND INTERACTIONS OF THE E.COLI CELL DIVISION ACTIVATOR PROTEIN CEDA===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_15865419}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[2bn8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BN8 OCA].
+</StructureSection>
 [[Category: Escherichia coli]]
 [[Category: Chen, H A.]]