View source for 6jtz


==Crystal Structure of hRecQ1_D2-Zn-WH containing mutation on beta-hairpin==
<StructureSection load='6jtz' size='340' side='right'caption='[[6jtz]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jtz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JTZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JTZ 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]] 2.797&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6jtz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jtz OCA], [https://pdbe.org/6jtz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jtz RCSB], [https://www.ebi.ac.uk/pdbsum/6jtz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jtz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RECQ1_HUMAN RECQ1_HUMAN] DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.<ref>PMID:15886194</ref> <ref>PMID:7961977</ref> <ref>PMID:8056767</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RECQ1 is the shortest among the five human RecQ helicases comprising of two RecA like domains, a zinc-binding domain and a RecQ C-terminal domain containing the winged-helix (WH). Mutations or deletions on the tip of a beta-hairpin located in the WH domain are known to abolish the unwinding activity. Interestingly, the same mutations on the beta-hairpin of annealing incompetent RECQ1 mutant (RECQ1T1) have been reported to restore its annealing activity. In an attempt to unravel the strand annealing mechanism, we have crystallized a fragment of RECQ1 encompassing D2-Zn-WH domains harbouring mutations on the beta-hairpin. From our crystal structure data and interface analysis, we have demonstrated that an alpha-helix located in zinc-binding domain potentially interacts with residues of WH domain, which plays a significant role in strand annealing activity. We have shown that deletion of the alpha-helix or mutation of specific residues on it restores strand annealing activity of annealing deficient constructs of RECQ1. Our results also demonstrate that mutations on the alpha-helix induce conformational changes and affects DNA stimulated ATP hydrolysis and unwinding activity of RECQ1. Our study, for the first time, provides insight into the conformational requirements of the WH domain for efficient strand annealing by human RECQ1.

Residues at the interface between zinc binding and winged helix domains of human RECQ1 play a significant role in DNA strand annealing activity.,Mukhopadhyay S, Das T, Bose M, Jain CK, Chakraborty M, Mukherjee S, Shikha K, Das AK, Ganguly A Nucleic Acids Res. 2021 Nov 18;49(20):11834-11854. doi: 10.1093/nar/gkab968. PMID:34751402<ref>PMID:34751402</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jtz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bose M]]
[[Category: Das AK]]
[[Category: Das T]]
[[Category: Ganguly A]]
[[Category: Mukhopadhyay S]]