9i16: Difference between revisions
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==Structure of RecQL-dsDNA-ADP-AlF4 complex from Bos taurus== | |||
<StructureSection load='9i16' size='340' side='right'caption='[[9i16]], [[Resolution|resolution]] 2.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9i16]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9I16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9I16 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]] 2.82Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9i16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9i16 OCA], [https://pdbe.org/9i16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9i16 RCSB], [https://www.ebi.ac.uk/pdbsum/9i16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9i16 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0JN36_BOVIN A0JN36_BOVIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
RECQ1, the most abundant RecQ helicase in human cells, is involved in telomere maintenance in ALT cells and plays a critical role in maintaining genomic integrity and stability. Here, we present five high-resolution crystal structures that systematically reveal a novel mechanism by which the RECQ1 helicase recognizes and regulates G-quadruplex (G4) DNA structures. Our results demonstrate that DNA binding induces intra-subunit rearrangement in RECQ1, transitioning it from a closed to an open conformation. This rearrangement alters the stability of the dimer interface. G4 recognition and unwinding are driven by coordinated interactions between the D1/D2 domains and the single-stranded DNA (ssDNA)-binding channel. This dual engagement aligns the G4 tetrad in a geometry favorable for unwinding. ATP hydrolysis facilitates ssDNA translocation, positioning the beta-hairpin to disrupt hydrogen bonds-unraveling G4 structures in a manner analogous to the unwinding of dsDNA. This study proposes a mechanistic model for RECQ1-mediated G4 unwinding and elucidates how RECQ1 recognizes and unwinds distinct DNA structures. | |||
Structural mechanism of RECQ1 helicase in unfolding G-quadruplexes compared with duplex DNA.,Song ZY, Zhang X, Ai X, Huang LY, Hou XM, Fosse P, Liu NN, Mauffret O, Rety S, Xi XG Nucleic Acids Res. 2025 Sep 5;53(17):gkaf877. doi: 10.1093/nar/gkaf877. PMID:40966504<ref>PMID:40966504</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9i16" style="background-color:#fffaf0;"></div> | ||
[[Category: Ai | == References == | ||
[[Category: | <references/> | ||
[[Category: Rety | __TOC__ | ||
[[Category: Song | </StructureSection> | ||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Ai X]] | |||
[[Category: Liu NN]] | |||
[[Category: Rety S]] | |||
[[Category: Song ZY]] | |||
[[Category: Xi XG]] | |||
