2pvi

PVUII ENDONUCLEASE COMPLEXED TO AN IODINATED COGNATE DNA

spinqualitylabelsall models 2pvi, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pvi is a 4 chain structure with sequence from Atcc 29905. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: C38 Activity: Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [T2P2_PROHU] Recognizes the double-stranded sequence CAGCTG and cleaves after G-3. Publication Abstract from PubMed In restriction-modification systems, cleavage of substrate sites in cellular DNA by the restriction endonuclease is prevented by the action of a cognate methyltransferase that acts on the same substrate sites. The PvuII restriction endonuclease (R.PvuII) has been structurally characterized in a complex with substrate DNA (Cheng et al., 1994) and as an apoenzyme (Athanasiadis et al., 1994). We report here a structure, determined to 1.9 A resolution by crystallography, of a complex between R.PvuII and iodinated DNA. The presence of an iodine at the 5-carbon of the methylatable cytosine results in the following changes in the protein: His84 moved away from the modified base; this movement was amplified in His85 and disrupts an intersubunit hydrogen bond; and the base modification disturbs the distribution of water molecules that associate with these histidine residues and the area of the scissile bond. Considering these observations, hypotheses are given as to why a similar oligonucleotide, where a methyl group resides on the 5-carbon of the methylatable cytosine, is slowly cleaved by R.PvuII (Rice et al., 1995). How is modification of the DNA substrate recognized by the PvuII restriction endonuclease?,Horton JR, Bonventre J, Cheng X Biol Chem. 1998 Apr-May;379(4-5):451-8. PMID:9628337 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Endonuclease 3D structures

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