By the same authors

From the same journal

CRYSTAL STRUCTURE OF PVUII ENDONUCLEASE REVEALS EXTENSIVE STRUCTURAL HOMOLOGIES TO ECORV

Research output: Contribution to journalArticle

Author(s)

  • A ATHANASIADIS
  • M VLASSI
  • D KOTSIFAKI
  • P A TUCKER
  • K S WILSON
  • M KOKKINIDIS

Department/unit(s)

Publication details

JournalNature Structural Biology
DatePublished - Jul 1994
Issue number7
Volume1
Number of pages7
Pages (from-to)469-475
Original languageEnglish

Abstract

The crystal structure of the dimeric PvuII restriction endonuclease (R.PvuII) has been determined at a resolution of 2.4 Angstrom. 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. 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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