View source for 4abx


==Crystal structure of Deinococcus radiodurans RecN coiled-coil domain==
<StructureSection load='4abx' size='340' side='right'caption='[[4abx]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4abx]] is a 4 chain structure with sequence from [https://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=4ABX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ABX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.041&#8491;</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=4abx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4abx OCA], [https://pdbe.org/4abx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4abx RCSB], [https://www.ebi.ac.uk/pdbsum/4abx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4abx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RECN_DEIRA RECN_DEIRA] May be involved in recombinational repair of damaged DNA.
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4abx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Deinococcus radiodurans R1]]
[[Category: Large Structures]]
[[Category: McSweeney S]]
[[Category: Pellegrino S]]
[[Category: Radzimanowski J]]
[[Category: Timmins J]]
[[Category: De Sanctis D]]