Abstract
The crystal structure of the dimeric PvuII restriction endonuclease (R.PvuII) has been determined at a resolution of 2.4Å. The protein has a mixed α/β architecture and consists of two subdomains. Despite a lack of sequence homology, extensive structural similarities exist between one R.PvuII subdomain and the DNA-binding subdomain of EcoRV endonuclease (R.EcoRV); the dimerization subdomains are unrelated. Whithin the similar domains, flexible segments of R.PvuII are topologically equivalent to the DNA-binding turns of R.EcoRV; potential catalytic residues can be deduced from the structural similarities to R.EcoRV. Conformational flexibility is important for the interaction with DNA. A possible classification of endonuclease structures on the basis of the positions of the scissile phosphates is discussed.
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Athanasiadis, A., Vlassi, M., Kotsifaki, D. et al. Crystal structure of PvuII endonuclease reveals extensive structural homologies to EcoRV. Nat Struct Mol Biol 1, 469–475 (1994). https://doi.org/10.1038/nsb0794-469
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DOI: https://doi.org/10.1038/nsb0794-469
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