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1pvu

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1pvu, resolution 2.40Å ()
Activity: Type II site-specific deoxyribonuclease, with EC number 3.1.21.4
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

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

Publication Abstract from PubMed

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

1pvu is a 2 chain structure with sequence from Proteus vulgaris. Full crystallographic information is available from OCA.

See Also

Reference

  • 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

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