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1DFM

Crystal structure of restriction endonuclease BGLII complexed with DNA 16-mer

1DFM の概要
エントリーDOI10.2210/pdb1dfm/pdb
関連するPDBエントリー1BHM 1D2I
分子名称DNA (5'-D(*TP*AP*TP*TP*AP*TP*AP*GP*AP*TP*CP*TP*AP*TP*AP*A)-3'), ENDONUCLEASE BGLII, CALCIUM ION, ... (4 entities in total)
機能のキーワードrestriction endonuclease, restriction enzyme, protein-dna complex, hydrolase-dna complex, hydrolase/dna
由来する生物種Bacillus subtilis
タンパク質・核酸の鎖数4
化学式量合計61934.12
構造登録者
Lukacs, C.M.,Kucera, R.,Schildkraut, I.,Aggarwal, A.K. (登録日: 1999-12-06, 公開日: 2000-02-21, 最終更新日: 2024-10-09)
主引用文献Lukacs, C.M.,Kucera, R.,Schildkraut, I.,Aggarwal, A.K.
Understanding the immutability of restriction enzymes: crystal structure of BglII and its DNA substrate at 1.5 A resolution.
Nat.Struct.Biol., 7:134-140, 2000
Cited by
PubMed Abstract: Restriction endonucleases are remarkably resilient to alterations in their DNA binding specificity. To understand the basis of this immutability, we have determined the crystal structure of endonuclease BglII bound to its recognition sequence (AGATCT), at 1. 5 A resolution. We compare the structure of BglII to endonuclease BamHI, which recognizes a closely related DNA site (GGATCC). We show that both enzymes share a similar alpha/beta core, but in BglII, the core is augmented by a beta-sandwich domain that encircles the DNA to provide extra specificity. Remarkably, the DNA is contorted differently in the two structures, leading to different protein-DNA contacts for even the common base pairs. Furthermore, the BglII active site contains a glutamine in place of the glutamate at the general base position in BamHI, and only a single metal is found coordinated to the putative nucleophilic water and the phosphate oxygens. This surprising diversity in structures shows that different strategies can be successful in achieving site-specific recognition and catalysis in restriction endonucleases.
PubMed: 10655616
DOI: 10.1038/72405
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.5 Å)
構造検証レポート
Validation report summary of 1dfm
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-03-04に公開中

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