View source for 8rxk


==ComM helicase from Legionella pneumophila, coordinating dsDNA and AMP-PNP==
<StructureSection load='8rxk' size='340' side='right'caption='[[8rxk]], [[Resolution|resolution]] 3.23&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8rxk]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RXK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.23&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=8rxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rxk OCA], [https://pdbe.org/8rxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rxk RCSB], [https://www.ebi.ac.uk/pdbsum/8rxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rxk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5ZXZ0_LEGPH Q5ZXZ0_LEGPH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Some DNA helicases play central and specific roles in genome maintenance and plasticity through their branch migration activity in different pathways of homologous recombination. RadA is a highly conserved bacterial helicase involved in DNA repair throughout all bacterial species. In Gram-positive Firmicutes, it also has a role in natural transformation, while in Gram-negative bacteria, ComM is the canonical transformation-specific helicase. Both RadA and ComM helicases form hexameric rings and use ATP hydrolysis as an energy source to propel themselves along DNA. In this study, we present the cryoEM structures of RadA and ComM interacting with DNA and ATP analogs. These structures reveal important molecular interactions that couple ATP hydrolysis and DNA binding in RadA, as well as the role of the Lon protease-like domain, shared by RadA and ComM, in this process. Taken together, these results provide new molecular insights into the mechanisms of DNA branch migration in different pathways of homologous recombination.

Structural insights into the mechanism of DNA branch migration during homologous recombination in bacteria.,Rosa LT, Vernhes E, Soulet AL, Polard P, Fronzes R EMBO J. 2024 Oct 18. doi: 10.1038/s44318-024-00264-5. PMID:39424952<ref>PMID:39424952</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8rxk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila]]
[[Category: Synthetic construct]]
[[Category: Fronzes R]]
[[Category: Talachia Rosa L]]