|1pvu, resolution 2.40Å ()|
THE CRYSTAL STRUCTURE OF PVUII ENDONUCLEASE REVEALS EXTENSIVE STRUCTURAL HOMOLOGIES TO ECORV
The crystal structure of the dimeric PvuII restriction endonuclease (R.PvuII) has been determined at a resolution of 2.4A. The protein has a mixed alpha/beta 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. Within 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.
Crystal structure of PvuII endonuclease reveals extensive structural homologies to EcoRV., Athanasiadis A, Vlassi M, Kotsifaki D, Tucker PA, Wilson KS, Kokkinidis M, Nat Struct Biol. 1994 Jul;1(7):469-75. PMID:7664066
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Athanasiadis A, Vlassi M, Kotsifaki D, Tucker PA, Wilson KS, Kokkinidis M. Crystal structure of PvuII endonuclease reveals extensive structural homologies to EcoRV. Nat Struct Biol. 1994 Jul;1(7):469-75. PMID:7664066