4U7D

Structure of human RECQ-like helicase in complex with an oligonucleotide

Summary for 4U7D

• Entry DOI: 10.2210/pdb4u7d/pdb
• Descriptor: ATP-dependent DNA helicase Q1, DNA oligonucleotide, ZINC ION (3 entities in total)
• Functional Keywords: hydrolase-dna complex, nuclear protein, hydrolase, dna strand annealing, dna binding protein, structural genomics, structural genomics consortium, sgc, hydrolase/dna
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : P46063
• Total number of polymer chains: 8
• Total formula weight: 294069.04

Authors

Pike, A.C.W.,Zhang, Y.,Schnecke, C.,Cooper, C.D.O.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.,Bountra, C.,Gileadi, O.,Structural Genomics Consortium (SGC) (deposition date: 2014-07-30, release date: 2015-01-21, Last modification date: 2024-10-23)

Primary citation

Pike, A.C.,Gomathinayagam, S.,Swuec, P.,Berti, M.,Zhang, Y.,Schnecke, C.,Marino, F.,von Delft, F.,Renault, L.,Costa, A.,Gileadi, O.,Vindigni, A.
Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: Insights from DNA complex structures.
Proc.Natl.Acad.Sci.USA, 112:4286-4291, 2015

PubMed Abstract: RecQ helicases are a widely conserved family of ATP-dependent motors with diverse roles in nearly every aspect of bacterial and eukaryotic genome maintenance. However, the physical mechanisms by which RecQ helicases recognize and process specific DNA replication and repair intermediates are largely unknown. Here, we solved crystal structures of the human RECQ1 helicase in complexes with tailed-duplex DNA and ssDNA. The structures map the interactions of the ssDNA tail and the branch point along the helicase and Zn-binding domains, which, together with reported structures of other helicases, define the catalytic stages of helicase action. We also identify a strand-separating pin, which (uniquely in RECQ1) is buttressed by the protein dimer interface. A duplex DNA-binding surface on the C-terminal domain is shown to play a role in DNA unwinding, strand annealing, and Holliday junction (HJ) branch migration. We have combined EM and analytical ultracentrifugation approaches to show that RECQ1 can form what appears to be a flat, homotetrameric complex and propose that RECQ1 tetramers are involved in HJ recognition. This tetrameric arrangement suggests a platform for coordinated activity at the advancing and receding duplexes of an HJ during branch migration.

PubMed: 25831490
DOI: 10.1073/pnas.1417594112

Experimental method

X-RAY DIFFRACTION (3.4 Å)