2owy
From Proteopedia
(Difference between revisions)
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<StructureSection load='2owy' size='340' side='right'caption='[[2owy]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='2owy' size='340' side='right'caption='[[2owy]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2owy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2owy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OWY FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=2owy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2owy OCA], [https://pdbe.org/2owy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2owy RCSB], [https://www.ebi.ac.uk/pdbsum/2owy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2owy ProSAT]</span></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=2owy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2owy OCA], [https://pdbe.org/2owy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2owy RCSB], [https://www.ebi.ac.uk/pdbsum/2owy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2owy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/RDGC_PSEAE RDGC_PSEAE] May be involved in recombination (By similarity). | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=2owy ConSurf]. | </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=2owy ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | RecA plays a central role in the nonmutagenic repair of stalled replication forks in bacteria. RdgC, a recombination-associated DNA-binding protein, is a potential negative regulator of RecA function. Here, we have determined the crystal structure of RdgC from Pseudomonas aeruginosa. The J-shaped monomer has a unique fold and can be divided into three structural domains: tip domain, center domain and base domain. Two such monomers dimerize to form a ring-shaped molecule of approximate 2-fold symmetry. Of the two inter-subunit interfaces within the dimer, one interface ('interface A') between tip/center domains is more nonpolar than the other ('interface B') between base domains. The structure allows us to propose that the RdgC dimer binds dsDNA through the central hole of approximately 30 A diameter. The proposed model is supported by our DNA-binding assays coupled with mutagenesis, which indicate that the conserved positively charged residues on the protein surface around the central hole play important roles in DNA binding. The novel ring-shaped architecture of the RdgC dimer has significant implications for its role in homologous recombination. | ||
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| - | The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding.,Ha JY, Kim HK, Kim do J, Kim KH, Oh SJ, Lee HH, Yoon HJ, Song HK, Suh SW Nucleic Acids Res. 2007;35(8):2671-81. Epub 2007 Apr 10. PMID:17426134<ref>PMID:17426134</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2owy" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Pseudomonas aeruginosa PAO1]] | |
| - | + | [[Category: Suh SW]] | |
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| - | [[Category: Pseudomonas aeruginosa]] | + | |
| - | [[Category: | + | |
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Current revision
The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding
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