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2owl
From Proteopedia
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| - | [[Image:2owl.gif|left|200px]] | ||
| - | + | ==Crystal structure of E. coli RdgC== | |
| - | + | <StructureSection load='2owl' size='340' side='right'caption='[[2owl]], [[Resolution|resolution]] 2.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2owl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OWL FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |
| - | --> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rdgC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2owl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2owl OCA], [https://pdbe.org/2owl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2owl RCSB], [https://www.ebi.ac.uk/pdbsum/2owl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2owl ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [[https://www.uniprot.org/uniprot/RDGC_ECOLI RDGC_ECOLI]] May be involved in recombination. | |
| - | == | + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ow/2owl_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2owl ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The DNA-binding protein, RdgC, is associated with recombination and replication fork repair in Escherichia coli and with the virulence-associated, pilin antigenic variation mediated by RecA and other recombination proteins in Neisseria species. We solved the structure of the E. coli protein and refined it to 2.4A. RdgC crystallizes as a dimer with a head-to-head, tail-to-tail organization forming a ring with a 30 A diameter hole at the center. The protein fold is unique and reminiscent of a horseshoe with twin gates closing the open end. The central hole is lined with positively charged residues and provides a highly plausible DNA binding channel consistent with the nonspecific mode of binding detected in vitro and with the ability of RdgC to modulate RecA function in vivo. | The DNA-binding protein, RdgC, is associated with recombination and replication fork repair in Escherichia coli and with the virulence-associated, pilin antigenic variation mediated by RecA and other recombination proteins in Neisseria species. We solved the structure of the E. coli protein and refined it to 2.4A. RdgC crystallizes as a dimer with a head-to-head, tail-to-tail organization forming a ring with a 30 A diameter hole at the center. The protein fold is unique and reminiscent of a horseshoe with twin gates closing the open end. The central hole is lined with positively charged residues and provides a highly plausible DNA binding channel consistent with the nonspecific mode of binding detected in vitro and with the ability of RdgC to modulate RecA function in vivo. | ||
| - | + | Ring structure of the Escherichia coli DNA-binding protein RdgC associated with recombination and replication fork repair.,Briggs GS, McEwan PA, Yu J, Moore T, Emsley J, Lloyd RG J Biol Chem. 2007 Apr 27;282(17):12353-7. Epub 2007 Feb 16. PMID:17308310<ref>PMID:17308310</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2owl" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Briggs, G S | + | <references/> |
| - | [[Category: Emsley, J | + | __TOC__ |
| - | [[Category: Lloyd, R G | + | </StructureSection> |
| - | [[Category: McEwan, P A | + | [[Category: Bacillus coli migula 1895]] |
| - | [[Category: Moore, T | + | [[Category: Large Structures]] |
| - | [[Category: Yu, J | + | [[Category: Briggs, G S]] |
| + | [[Category: Emsley, J]] | ||
| + | [[Category: Lloyd, R G]] | ||
| + | [[Category: McEwan, P A]] | ||
| + | [[Category: Moore, T]] | ||
| + | [[Category: Yu, J]] | ||
[[Category: Reca]] | [[Category: Reca]] | ||
[[Category: Recombination]] | [[Category: Recombination]] | ||
[[Category: Replication]] | [[Category: Replication]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:48:57 2008'' | ||
Current revision
Crystal structure of E. coli RdgC
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