4TMU

Crystal structure of RecQ catalytic core from C. sakazakii bound to DNA

Summary for 4TMU

• Entry DOI: 10.2210/pdb4tmu/pdb
• Descriptor: RecQ, DNA (29-MER), ZINC ION, ... (4 entities in total)
• Functional Keywords: recq, helicase, winged helix, atp binding, hydrolase-dna complex, hydrolase/dna
• Biological source: Cronobacter sakazakii; More
• Total number of polymer chains: 2
• Total formula weight: 70959.40

Authors

Manthei, K.A.,Keck, J.L. (deposition date: 2014-06-02, release date: 2015-03-11, Last modification date: 2023-12-27)

Primary citation

Manthei, K.A.,Hill, M.C.,Burke, J.E.,Butcher, S.E.,Keck, J.L.
Structural mechanisms of DNA binding and unwinding in bacterial RecQ helicases.
Proc.Natl.Acad.Sci.USA, 112:4292-4297, 2015

PubMed Abstract: RecQ helicases unwind remarkably diverse DNA structures as key components of many cellular processes. How RecQ enzymes accommodate different substrates in a unified mechanism that couples ATP hydrolysis to DNA unwinding is unknown. Here, the X-ray crystal structure of the Cronobacter sakazakii RecQ catalytic core domain bound to duplex DNA with a 3' single-stranded extension identifies two DNA-dependent conformational rearrangements: a winged-helix domain pivots ∼90° to close onto duplex DNA, and a conserved aromatic-rich loop is remodeled to bind ssDNA. These changes coincide with a restructuring of the RecQ ATPase active site that positions catalytic residues for ATP hydrolysis. Complex formation also induces a tight bend in the DNA and melts a portion of the duplex. This bending, coupled with translocation, could provide RecQ with a mechanism for unwinding duplex and other DNA structures.

PubMed: 25831501
DOI: 10.1073/pnas.1416746112

Experimental method

X-RAY DIFFRACTION (2.4 Å)