6jtz

Crystal Structure of hRecQ1_D2-Zn-WH containing mutation on beta-hairpin

spinqualitylabelsall models 6jtz, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jtz is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.797Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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