7OTJ

Crystal structure of Pif1 helicase from Candida albicans

Summary for 7OTJ

• Entry DOI: 10.2210/pdb7otj/pdb
• Descriptor: ATP-dependent DNA helicase PIF1, DNA (5'-D(P*TP*TP*TP*TP*TP*T)-3'), ADENOSINE-5'-DIPHOSPHATE, ... (8 entities in total)
• Functional Keywords: helicase pif1, hydrolase
• Biological source: Candida albicans; More
• Total number of polymer chains: 4
• Total formula weight: 122334.71

Authors

Rety, S.,Xi, X.G. (deposition date: 2021-06-10, release date: 2021-07-07, Last modification date: 2024-01-31)

Primary citation

Lu, K.Y.,Xin, B.G.,Zhang, T.,Liu, N.N.,Li, D.,Rety, S.,Xi, X.G.
Structural study of the function of Candida Albicans Pif1.
Biochem.Biophys.Res.Commun., 567:190-194, 2021

PubMed Abstract: Pif1 helicases, conserved in eukaryotes, are involved in maintaining genome stability in both the nucleus and mitochondria. Here, we report the crystal structure of a truncated Candida Albicans Pif1 (CaPif1) in complex with ssDNA and an ATP analog. Our results show that the Q-motif is responsible for identifying adenine bases, and CaPif1 preferentially utilizes ATP/dATP during dsDNA unwinding. Although CaPif1 shares structural similarities with Saccharomyces cerevisiae Pif1, CaPif1 can contact the thymidine bases of DNA by hydrogen bonds, whereas ScPif1 cannot. More importantly, the crosslinking and mutant experiments have demonstrated that the conformational change of domain 2B is necessary for CaPif1 to unwind dsDNA. These findings contribute to further the understanding of the unwinding mechanism of Pif1.

PubMed: 34166917
DOI: 10.1016/j.bbrc.2021.06.050

Experimental method

X-RAY DIFFRACTION (2.58 Å)