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2bn8
From Proteopedia
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| - | [[Image:2bn8.jpg|left|200px]]<br /><applet load="2bn8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | 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== |
| + | <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. | ||
| + | <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. | 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> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2bn8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Chen | + | [[Category: Chen HA]] |
| - | [[Category: Huyton | + | [[Category: Huyton T]] |
| - | [[Category: Matthews | + | [[Category: Matthews S]] |
| - | [[Category: Roper | + | [[Category: Roper D]] |
| - | [[Category: Simpson | + | [[Category: Simpson P]] |
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Current revision
Solution Structure and interactions of the E .coli Cell Division Activator Protein CedA
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