1DMU

Crystal structure of the restriction endonuclease BglI (e.c.3.1.21.4) bound to its dna recognition sequence

1DMU の概要

• エントリーDOI: 10.2210/pdb1dmu/pdb
• 分子名称: DNA (5'-D(*AP*TP*CP*GP*CP*CP*TP*AP*AP*TP*AP*GP*GP*CP*GP*AP*T)-3'), BGLI RESTRICTION ENDONUCLEASE, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: protein-dna complex, active site calcium ions, alpha/beta structure, a:a mismatch, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Bacillus subtilis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39500.64

構造登録者

Newman, M.,Lunnen, K.,Wilson, G.,Greci, J.,Schildkraut, I.,Phillips, S.E.V. (登録日: 1999-12-15, 公開日: 1999-12-18, 最終更新日: 2021-02-03)

主引用文献

Newman, M.,Lunnen, K.,Wilson, G.,Greci, J.,Schildkraut, I.,Phillips, S.E.
Crystal structure of restriction endonuclease BglI bound to its interrupted DNA recognition sequence.
EMBO J., 17:5466-5476, 1998

PubMed Abstract: The crystal structure of the type II restriction endonuclease BglI bound to DNA containing its specific recognition sequence has been determined at 2.2 A resolution. This is the first structure of a restriction endonuclease that recognizes and cleaves an interrupted DNA sequence, producing 3' overhanging ends. BglI is a homodimer that binds its specific DNA sequence with the minor groove facing the protein. Parts of the enzyme reach into both the major and minor grooves to contact the edges of the bases within the recognition half-sites. The arrangement of active site residues is strikingly similar to other restriction endonucleases, but the co-ordination of two calcium ions at the active site gives new insight into the catalytic mechanism. Surprisingly, the core of a BglI subunit displays a striking similarity to subunits of EcoRV and PvuII, but the dimer structure is dramatically different. The BglI-DNA complex demonstrates, for the first time, that a conserved subunit fold can dimerize in more than one way, resulting in different DNA cleavage patterns.

PubMed: 9736624
DOI: 10.1093/emboj/17.18.5466

実験手法

X-RAY DIFFRACTION (2.2 Å)