1P8K

The structure and DNA recognition of a bifunctional homing endonuclease and group I intron splicing factor

1P8K の概要

• エントリーDOI: 10.2210/pdb1p8k/pdb
• 分子名称: 5'-D(P*GP*CP*GP*CP*GP*CP*TP*GP*AP*GP*GP*AP*GP*GP*TP*TP*TP*C)-3', 5'-D(P*TP*CP*TP*GP*TP*AP*AP*AP*GP*CP*GP*CP*A)-3', 5'-D(P*GP*CP*GP*CP*TP*TP*TP*AP*CP*AP*GP*AP*GP*AP*AP*A)-3', ... (6 entities in total)
• 機能のキーワード: hydrolase/dna, hydrolase-dna complex
• 由来する生物種: Emericella nidulans
• 細胞内の位置: Mitochondrion: P03880
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 48641.10

構造登録者

Stoddard, B.L.,Bolduc, J.M. (登録日: 2003-05-07, 公開日: 2004-01-20, 最終更新日: 2024-11-20)

主引用文献

Bolduc, J.M.,Spiegel, P.C.,Chatterjee, P.,Brady, K.L.,Downing, M.E.,Caprara, M.G.,Waring, R.B.,Stoddard, B.L.
Structural and biochemical analyses of DNA and RNA binding by a bifunctional homing endonuclease and group I intron splicing factor.
Genes Dev., 17:2875-2888, 2003

PubMed Abstract: We determined the crystal structure of a bifunctional group I intron splicing factor and homing endonuclease, termed the I-AniI maturase, in complex with its DNA target at 2.6 A resolution. The structure demonstrates the remarkable structural conservation of the beta-sheet DNA-binding motif between highly divergent enzyme subfamilies. DNA recognition by I-AniI was further studied using nucleoside deletion and DMS modification interference analyses. Correlation of these results with the crystal structure provides information on the relative importance of individual nucleotide contacts for DNA recognition. Alignment and modeling of two homologous maturases reveals conserved basic surface residues, distant from the DNA-binding surface, that might be involved in RNA binding. A point mutation that introduces a single negative charge in this region uncouples the maturase and endonuclease functions of the protein, inhibiting RNA binding and splicing while maintaining DNA binding and cleavage.

PubMed: 14633971
DOI: 10.1101/gad.1109003

実験手法

X-RAY DIFFRACTION (2.6 Å)