2e6l

Structural highlights

Function

WRN_MOUSE Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity).^{[1] [2]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Helicase 3D structures

References

1. ↑ Lombard DB, Beard C, Johnson B, Marciniak RA, Dausman J, Bronson R, Buhlmann JE, Lipman R, Curry R, Sharpe A, Jaenisch R, Guarente L. Mutations in the WRN gene in mice accelerate mortality in a p53-null background. Mol Cell Biol. 2000 May;20(9):3286-91. PMID:10757812
2. ↑ Choi JM, Kang SY, Bae WJ, Jin KS, Ree M, Cho Y. Probing the roles of active site residues in the 3'-5' exonuclease of the Werner syndrome protein. J Biol Chem. 2007 Mar 30;282(13):9941-51. Epub 2007 Jan 16. PMID:17229737 doi:10.1074/jbc.M609657200