View source for 5loi


==Crystal structure of Myceliophthora thermophila Rad26 (residues 373-841)==
<StructureSection load='5loi' size='340' side='right'caption='[[5loi]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5loi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothelomyces_thermophilus_ATCC_42464 Thermothelomyces thermophilus ATCC 42464]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LOI 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]] 3.153&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5loi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loi OCA], [https://pdbe.org/5loi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5loi RCSB], [https://www.ebi.ac.uk/pdbsum/5loi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5loi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G2QDY6_MYCTT G2QDY6_MYCTT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metabolic products and environmental factors constantly damage DNA. To protect against these insults and maintain genome integrity, cells have evolved mechanisms to repair DNA lesions. One such mechanism involves Rad3, a master kinase coordinating the DNA damage response. Rad26 is a functional subunit of the Rad3-Rad26 complex and responsible for bringing the kinase to sites of DNA damage. Here, I present the crystal structure of Rad26 and identify the elements important for recruiting Rad3. The structure suggests that Rad26 is a dimer with a conserved interface in the N-terminal part of the protein. Biochemical data shows that Rad26 uses its C-terminal domain and the flanking kinase-docking motif to bind specific HEAT repeats in Rad3. Analysis of the reconstituted Rad3-Rad26 heterotetrameric complex with electron microscopy enabled me to propose a structural model for its quaternary structure. In conclusion, these results suggest that Rad26 exists as a dimer and provide crucial insight into how Rad3 is recruited and incorporated into the Rad3-Rad26 DNA repair complex.

Insights into Rad3 kinase recruitment from the crystal structure of the DNA damage checkpoint protein Rad26.,Andersen KR J Biol Chem. 2017 Mar 17. pii: jbc.M117.780189. doi: 10.1074/jbc.M117.780189. PMID:28314775<ref>PMID:28314775</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5loi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermothelomyces thermophilus ATCC 42464]]
[[Category: Andersen KR]]