Structural highlights
Function
[T2P2_PROHU] Recognizes the double-stranded sequence CAGCTG and cleaves after G-3.
Publication Abstract from PubMed
The restriction endonuclease PvuII from Proteus vulgaris has been converted from its wild-type homodimeric form into the enzymatically active single-chain variant scPvuII by tandemly joining the two subunits through the peptide linker Gly-Ser-Gly-Gly. scPvuII, which is suitable for the development of programmed restriction endonucleases for highly specific DNA cleavage, was purified and crystallized. The crystals diffract to a resolution of 2.35 A and belong to space group P4(2), with unit-cell parameters a = b = 101.92, c = 100.28 A and two molecules per asymmetric unit. Phasing was successfully performed by molecular replacement.
Purification, crystallization, X-ray diffraction analysis and phasing of an engineered single-chain PvuII restriction endonuclease.,Meramveliotaki C, Kotsifaki D, Androulaki M, Hountas A, Eliopoulos E, Kokkinidis M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):836-8. Epub 2007 Sep 19. PMID:17909283[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Meramveliotaki C, Kotsifaki D, Androulaki M, Hountas A, Eliopoulos E, Kokkinidis M. Purification, crystallization, X-ray diffraction analysis and phasing of an engineered single-chain PvuII restriction endonuclease. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):836-8. Epub 2007 Sep 19. PMID:17909283 doi:10.1107/S1744309107040377
