1996
DOI: 10.1126/science.274.5286.415
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Crystal Structure of DNA Recombination Protein RuvA and a Model for Its Binding to the Holliday Junction

Abstract: The Escherichia coli DNA binding protein RuvA acts in concert with the helicase RuvB to drive branch migration of Holliday intermediates during recombination and DNA repair. The atomic structure of RuvA was determined at a resolution of 1.9 angstroms. Four monomers of RuvA are related by fourfold symmetry in a manner reminiscent of a four-petaled flower. The four DNA duplex arms of a Holliday junction can be modeled in a square planar configuration and docked into grooves on the concave surface of the protein … Show more

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Cited by 166 publications
(165 citation statements)
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“…Crystallographic studies have revealed a three-dimensional structure of a RuvA tetramer in which four monomers of RuvA are related by a fourfold symmetry (Rafferty et al 1996;Nishino et al 1998). A model of the RuvA-Holliday junction complex which was constructed from the RuvA crystal structure is consistent with the above branch migration mechanism hypothesis (Rafferty et al 1996).…”
Section: Introductionmentioning
confidence: 59%
“…Crystallographic studies have revealed a three-dimensional structure of a RuvA tetramer in which four monomers of RuvA are related by a fourfold symmetry (Rafferty et al 1996;Nishino et al 1998). A model of the RuvA-Holliday junction complex which was constructed from the RuvA crystal structure is consistent with the above branch migration mechanism hypothesis (Rafferty et al 1996).…”
Section: Introductionmentioning
confidence: 59%
“…1B). On the extensive basic surface of the RuvA tetramer, eight residues, corresponding to Glu-55 and Asp-56 in each subunit, form an acidic central pin (9) (Fig. 2D).…”
Section: Resultsmentioning
confidence: 99%
“…Crystallographic and biochemical studies revealed that RuvA adopts a unique tetrameric architecture formed by identical subunits with three distinct domains (9,10). Proteolytic and mutational analyses demonstrated that domain III plays a major role in the ATP-dependent branch migration through direct contact with RuvB whereas the remaining major core (I and II) is responsible for Holliday junction binding (10,11).…”
mentioning
confidence: 99%
“…RuvA has four acidic pins that are probably involved in strand separation, although they do not take up space in the center of the HJ (41). Peptide WRWYCR does not prevent a RuvA tetramer from binding to HJ substrates (K.V.K.…”
Section: Discussionmentioning
confidence: 99%