5z69: Difference between revisions
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The | ==Structure of the recombination mediator protein RecF-ATPrS in RecFOR pathway== | ||
<StructureSection load='5z69' size='340' side='right' caption='[[5z69]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5z69]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z69 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z69 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene></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=5z69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z69 OCA], [http://pdbe.org/5z69 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z69 RCSB], [http://www.ebi.ac.uk/pdbsum/5z69 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z69 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/RECF_CALS4 RECF_CALS4]] The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
RecF is a principal member of the RecF pathway. It interacts with RecO and RecR to initiate homologous recombination by loading RecA recombinases on single-stranded DNA and displacing single-stranded DNA-binding proteins. As an ATP-binding cassette ATPase, RecF exhibits ATP-dependent dimerization and structural homology with Rad50 and SMC proteins. However, the mechanism and action pattern of RecF ATP-dependent dimerization remains unclear. Here, We determined three crystal structures of TTERecF, TTERecF-ATP and TTERecF-ATPS from Thermoanaerobacter tengcongensis that reveal a novel ATP-driven RecF dimerization. RecF contains a positively charged tunnel on its dimer interface that is essential to ATP binding. Our structural and biochemical data indicate that the Walker A motif serves as a switch and plays a key role in ATP binding and RecF dimerization. Furthermore, Biolayer interferometry assay results showed that the TTERecF interacted with ATP and formed a dimer, displaying a higher affinity for DNA than that of the TTERecF monomer. Overall, our results provide a solid structural basis for understanding the process of RecF binding with ATP and the functional mechanism of ATP-dependent RecF dimerization. | |||
ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair.,Tang Q, Liu YP, Shan HH, Tian LF, Zhang JZ, Yan XX Sci Rep. 2018 Feb 1;8(1):2127. doi: 10.1038/s41598-018-20557-0. PMID:29391496<ref>PMID:29391496</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5z69" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Liu, Y P]] | |||
[[Category: Tang, Q]] | [[Category: Tang, Q]] | ||
[[Category: Yan, X | [[Category: Yan, X X]] | ||
[[Category: | [[Category: Dna binding protein]] | ||
[[Category: Dna repair]] | |||
[[Category: Rad50]] | |||
[[Category: Recf]] | |||
[[Category: Recfor]] | |||
[[Category: Recombination mediator]] | |||
