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Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction.

Rafferty, J.B.; Sedelnikova, S.E.; Hargreaves, D.; Artymiuk, P.J.; Baker, P.J.; Sharples, G.J.; Mahdi, A.A.; Lloyd, R.G.; Rice, D.W.

Authors

J.B. Rafferty

S.E. Sedelnikova

D. Hargreaves

P.J. Artymiuk

P.J. Baker

A.A. Mahdi

R.G. Lloyd

D.W. Rice



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 around a central pin that may facilitate strand separation during the migration reaction. The model presented reveals how a RuvAB-junction complex may also accommodate the resolvase RuvC.

Citation

Rafferty, J., Sedelnikova, S., Hargreaves, D., Artymiuk, P., Baker, P., Sharples, G., …Rice, D. (1996). Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. Science, 274(5286), 415-421

Journal Article Type Article
Publication Date 1996
Journal Science
Print ISSN 0036-8075
Publisher American Association for the Advancement of Science
Volume 274
Issue 5286
Pages 415-421
Publisher URL http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8832889