View source for 2bn8


==Solution Structure and interactions of the E .coli Cell Division Activator Protein CedA==
<StructureSection load='2bn8' size='340' side='right'caption='[[2bn8]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bn8]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2BN8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bn8 OCA], [https://pdbe.org/2bn8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bn8 RCSB], [https://www.ebi.ac.uk/pdbsum/2bn8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bn8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CEDA_ECOLI CEDA_ECOLI] Activates the cell division inhibited by chromosomal DNA over-replication.
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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Chen HA]]
[[Category: Huyton T]]
[[Category: Matthews S]]
[[Category: Roper D]]
[[Category: Simpson P]]