1CUK
ESCHERICHIA COLI RUVA PROTEIN AT PH 4.9 AND ROOM TEMPERATURE
Summary for 1CUK
| Entry DOI | 10.2210/pdb1cuk/pdb |
| Descriptor | RUVA PROTEIN (2 entities in total) |
| Functional Keywords | dna repair, sos response, dna-binding, dna recombination, helicase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 22197.78 |
| Authors | Rafferty, J.B.,Rice, D.W. (deposition date: 1996-08-28, release date: 1997-10-22, Last modification date: 2024-02-07) |
| Primary citation | 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. Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. Science, 274:415-421, 1996 Cited by PubMed 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. PubMed: 8832889DOI: 10.1126/science.274.5286.415 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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