2PVI

PVUII ENDONUCLEASE COMPLEXED TO AN IODINATED COGNATE DNA

2PVI の概要

• エントリーDOI: 10.2210/pdb2pvi/pdb
• 分子名称: DNA (5'-D(*TP*GP*AP*CP*CP*AP*GP*(C38)P*TP*GP*GP*TP*C)-3'), TYPE II RESTRICTION ENZYME PVUII (3 entities in total)
• 機能のキーワード: complex (restriction endonuclease-dna), hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Proteus vulgaris
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44628.68

構造登録者

Horton, J.,Cheng, X. (登録日: 1998-11-01, 公開日: 1999-12-20, 最終更新日: 2023-08-30)

主引用文献

Horton, J.R.,Bonventre, J.,Cheng, X.
How is modification of the DNA substrate recognized by the PvuII restriction endonuclease?
J.Biol.Chem., 379:451-458, 1998

PubMed Abstract: 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).

PubMed: 9628337

実験手法

X-RAY DIFFRACTION (1.76 Å)