4aby
From Proteopedia
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| - | [[ | + | ==Crystal structure of Deinococcus radiodurans RecN head domain== |
| + | <StructureSection load='4aby' size='340' side='right' caption='[[4aby]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4aby]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans_r1 Deinococcus radiodurans r1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ABY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ABY FirstGlance]. <br> | ||
| + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4abx|4abx]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosinetriphosphatase Adenosinetriphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.3 3.6.1.3] </span></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=4aby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aby OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4aby RCSB], [http://www.ebi.ac.uk/pdbsum/4aby PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Repair of DNA double-strand breaks (DSBs) is essential for cell survival and maintaining genome integrity. DSBs are repaired in a stepwise manner by homologous recombination. Here, we focused on the early steps of DSB repair, including DSB recognition, which is still only poorly understood. In prokaryotes, this process has been proposed to involve the RecN protein, a member of the structural maintenance of chromosome (SMC) protein family, which include key eukaryotic and prokaryotic proteins such as cohesin, condensin, and Rad50. An extensive high- and low-resolution structural analysis of Deinococcus radiodurans RecN using a combination of protein crystallography and small-angle X-ray scattering enabled us to assemble a quasi-atomic model of the entire RecN protein, representing the complete structure of a SMC-like protein. These results, together with a thorough biochemical and mutational study of RecN, allow us to propose a model for the role of RecN in DSB repair. | ||
| - | + | Structural and Functional Characterization of an SMC-like Protein RecN: New Insights into Double-Strand Break Repair.,Pellegrino S, Radzimanowski J, de Sanctis D, Boeri Erba E, McSweeney S, Timmins J Structure. 2012 Dec 5;20(12):2076-89. doi: 10.1016/j.str.2012.09.010. Epub 2012, Oct 18. PMID:23085075<ref>PMID:23085075</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Adenosinetriphosphatase]] | [[Category: Adenosinetriphosphatase]] | ||
[[Category: Deinococcus radiodurans r1]] | [[Category: Deinococcus radiodurans r1]] | ||
| - | [[Category: Mcsweeney, S | + | [[Category: Mcsweeney, S]] |
| - | [[Category: Pellegrino, S | + | [[Category: Pellegrino, S]] |
| - | [[Category: Radzimanowski, J | + | [[Category: Radzimanowski, J]] |
| - | [[Category: Sanctis, D De | + | [[Category: Sanctis, D De]] |
| - | [[Category: Timmins, J | + | [[Category: Timmins, J]] |
[[Category: Atpase]] | [[Category: Atpase]] | ||
[[Category: Dna repair]] | [[Category: Dna repair]] | ||
Revision as of 15:54, 9 December 2014
Crystal structure of Deinococcus radiodurans RecN head domain
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