3AAF

Structure of WRN RQC domain bound to double-stranded DNA

Summary for 3AAF

• Entry DOI: 10.2210/pdb3aaf/pdb
• Descriptor: Werner syndrome ATP-dependent helicase, DNA (5'-D(*AP*CP*CP*CP*TP*AP*AP*TP*TP*AP*GP*GP*GP*T)-3'), ACETATE ION, ... (4 entities in total)
• Functional Keywords: helix-turn-helix, winged-helix, protein-dna complex, dna-binding, helicase, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus, nucleolus : Q14191
• Total number of polymer chains: 4
• Total formula weight: 39380.79

Authors

Kitano, K.,Hakoshima, T. (deposition date: 2009-11-16, release date: 2010-02-16, Last modification date: 2024-03-13)

Primary citation

Kitano, K.,Kim, S.Y.,Hakoshima, T.
Structural basis for DNA strand separation by the unconventional winged-helix domain of RecQ helicase WRN
Structure, 18:177-187, 2010

PubMed Abstract: The RecQ family of DNA helicases including WRN (Werner syndrome protein) and BLM (Bloom syndrome protein) protects the genome against deleterious changes. Here we report the cocrystal structure of the RecQ C-terminal (RQC) domain of human WRN bound to a DNA duplex. In the complex, the RQC domain specifically interacted with a blunt end of the duplex and, surprisingly, unpaired a Watson-Crick base pair in the absence of an ATPase domain. The beta wing, an extended hairpin motif that is characteristic of winged-helix motifs, was used as a "separating knife" to wedge between the first and second base pairs, whereas the recognition helix, a principal component of helix-turn-helix motifs that are usually embedded within DNA grooves, was unprecedentedly excluded from the interaction. Our results demonstrate a function of the winged-helix motif central to the helicase reaction, establishing the first structural paradigm concerning the DNA structure-specific activities of the RecQ helicases.

PubMed: 20159463
DOI: 10.1016/j.str.2009.12.011

Experimental method

X-RAY DIFFRACTION (1.9 Å)