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| - | ==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=''> | + | ==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 == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bn8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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> | + | <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='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://pdbe.org/2bn8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bn8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bn8 PDBsum]</span></td></tr> | + | </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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CEDA_ECOLI CEDA_ECOLI]] Activates the cell division inhibited by chromosomal DNA over-replication. | + | [https://www.uniprot.org/uniprot/CEDA_ECOLI CEDA_ECOLI] Activates the cell division inhibited by chromosomal DNA over-replication. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Chen, H A]] | + | [[Category: Large Structures]] |
| - | [[Category: Huyton, T]] | + | [[Category: Chen HA]] |
| - | [[Category: Matthews, S]] | + | [[Category: Huyton T]] |
| - | [[Category: Roper, D]] | + | [[Category: Matthews S]] |
| - | [[Category: Simpson, P]] | + | [[Category: Roper D]] |
| - | [[Category: Ceda]]
| + | [[Category: Simpson P]] |
| - | [[Category: Cell cycle protein]]
| + | |
| - | [[Category: Cell division activator protein]]
| + | |
| Structural highlights
Function
CEDA_ECOLI Activates the cell division inhibited by chromosomal DNA over-replication.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen HA, Simpson P, Huyton T, Roper D, Matthews S. Solution structure and interactions of the Escherichia coli cell division activator protein CedA. Biochemistry. 2005 May 10;44(18):6738-44. PMID:15865419 doi:http://dx.doi.org/10.1021/bi0500269
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