1M5X

Crystal structure of the homing endonuclease I-MsoI bound to its DNA substrate

1M5X の概要

• エントリーDOI: 10.2210/pdb1m5x/pdb
• 分子名称: 5'-D(*GP*CP*AP*GP*AP*AP*CP*GP*TP*CP*GP*TP*GP*AP*GP*AP*CP*AP*GP*TP*TP*CP*CP*G)-3', 5'-D(*CP*GP*GP*AP*AP*CP*TP*GP*TP*CP*TP*CP*AP*CP*GP*AP*CP*GP*TP*TP*CP*TP*GP*C)-3', DNA endonuclease I-MsoI, ... (5 entities in total)
• 機能のキーワード: laglidadg, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Monomastix sp.
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 53804.57

構造登録者

Chevalier, B.,Turmel, M.,Lemieux, C.,Monnat, R.J.,Stoddard, B.L. (登録日: 2002-07-10, 公開日: 2003-06-03, 最終更新日: 2024-04-03)

主引用文献

Chevalier, B.,Turmel, M.,Lemieux, C.,Monnat, R.J.,Stoddard, B.L.
Flexible DNA Target Site Recognition by Divergent Homing Endonuclease Isoschizomers I-CreI and I-MsoI
J.Mol.Biol., 329:253-269, 2003

PubMed Abstract: Homing endonucleases are highly specific catalysts of DNA strand breaks that induce the transposition of mobile intervening sequences containing the endonuclease open reading frame. These enzymes recognize long DNA targets while tolerating individual sequence polymorphisms within those sites. Sequences of the homing endonucleases themselves diversify to a great extent after founding intron invasion events, generating highly divergent enzymes that recognize similar target sequences. Here, we visualize the mechanism of flexible DNA recognition and the pattern of structural divergence displayed by two homing endonuclease isoschizomers. We determined structures of I-CreI bound to two DNA target sites that differ at eight of 22 base-pairs, and the structure of an isoschizomer, I-MsoI, bound to a nearly identical DNA target site. This study illustrates several principles governing promiscuous base-pair recognition by DNA-binding proteins, and demonstrates that the isoschizomers display strikingly different protein/DNA contacts. The structures allow us to determine the information content at individual positions in the binding site as a function of the distribution of direct and water-mediated contacts to nucleotide bases, and provide an evolutionary snapshot of endonucleases at an early stage of divergence in their target specificity.

PubMed: 12758074
DOI: 10.1016/S0022-2836(03)00447-9

実験手法

X-RAY DIFFRACTION (2.25 Å)