1PVU

THE CRYSTAL STRUCTURE OF PVUII ENDONUCLEASE REVEALS EXTENSIVE STRUCTURAL HOMOLOGIES TO ECORV

Summary for 1PVU

• Entry DOI: 10.2210/pdb1pvu/pdb
• Descriptor: Pvu II (2 entities in total)
• Functional Keywords: type ii restriction endonuclease
• Biological source: Proteus vulgaris
• Total number of polymer chains: 2
• Total formula weight: 36479.60

Authors

Vlassi, M.,Athanasiadis, A. (deposition date: 1995-03-09, release date: 1995-03-31, Last modification date: 2024-02-14)

Primary citation

Athanasiadis, A.,Vlassi, M.,Kotsifaki, D.,Tucker, P.A.,Wilson, K.S.,Kokkinidis, M.
Crystal structure of PvuII endonuclease reveals extensive structural homologies to EcoRV.
Nat.Struct.Biol., 1:469-475, 1994

PubMed Abstract: 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.

PubMed: 7664066
DOI: 10.1038/nsb0794-469

Experimental method

X-RAY DIFFRACTION (2.4 Å)