1LWT

Crystal structure of the intein homing endonuclease PI-SceI bound to its substrate DNA (Ca2+ free)

1LWT の概要

• エントリーDOI: 10.2210/pdb1lwt/pdb
• 関連するPDBエントリー: 1LWS 1VDE
• 分子名称: PI-SceI DNA substrate top strand, PI-SceI DNA substrate bottom strand, ENDONUCLEASE PI-SCEI, ... (4 entities in total)
• 機能のキーワード: homing endonuclease, protein-dna complex, intein, endonuclease, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Endomembrane system: P17255
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 74150.70

構造登録者

Moure, C.M.,Gimble, F.S.,Quiocho, F.A. (登録日: 2002-06-03, 公開日: 2002-09-27, 最終更新日: 2024-10-09)

主引用文献

Moure, C.M.,Gimble, F.S.,Quiocho, F.A.
Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence.
Nat.Struct.Biol., 9:764-770, 2002

PubMed Abstract: The first X-ray structures of an intein-DNA complex, that of the two-domain homing endonuclease PI-SceI bound to its 36-base pair DNA substrate, have been determined in the presence and absence of Ca(2+). The DNA shows an asymmetric bending pattern, with a major 50 degree bend in the endonuclease domain and a minor 22 degree bend in the splicing domain region. Distortions of the DNA bound to the endonuclease domain cause the insertion of the two cleavage sites in the catalytic center. DNA binding induces changes in the protein conformation. The two overlapping non-identical active sites in the endonucleolytic center contain two Ca(+2) ions that coordinate to the catalytic Asp residues. Structure analysis indicates that the top strand may be cleaved first.

PubMed: 12219083
DOI: 10.1038/nsb840

実験手法

X-RAY DIFFRACTION (3.2 Å)