1OMH

Conjugative Relaxase TrwC in complex with OriT Dna. Metal-free structure.

1OMH の概要

• エントリーDOI: 10.2210/pdb1omh/pdb
• 分子名称: DNA OLIGONUCLEOTIDE, trwC protein, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: protein-dna complex, bacterial conjugation, relaxase, dna replication, transferase-dna complex, transferase/dna
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41085.57

構造登録者

Guasch, A.,Lucas, M.,Moncalian, G.,Cabezas, M.,Perez-Luque, R.,Gomis-Ruth, F.X.,de la Cruz, F.,Coll, M. (登録日: 2003-02-25, 公開日: 2003-11-25, 最終更新日: 2024-10-30)

主引用文献

Guasch, A.,Lucas, M.,Moncalian, G.,Cabezas, M.,Perez-Luque, R.,Gomis-Ruth, F.X.,de la Cruz, F.,Coll, M.
Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC.
Nat.Struct.Biol., 10:1002-1010, 2003

PubMed Abstract: Relaxases are DNA strand transferases that catalyze the initial and final stages of DNA processing during conjugative cell-to-cell DNA transfer. Upon binding to the origin of transfer (oriT) DNA, relaxase TrwC melts the double helix. The three-dimensional structure of the relaxase domain of TrwC in complex with its cognate DNA at oriT shows a fold built on a two-layer alpha/beta sandwich, with a deep narrow cleft that houses the active site. The DNA includes one arm of an extruded cruciform, an essential feature for specific recognition. This arm is firmly embraced by the protein through a beta-ribbon positioned in the DNA major groove and a loop occupying the minor groove. It is followed by a single-stranded DNA segment that enters the active site, after a sharp U-turn forming a hydrophobic cage that traps the N-terminal methionine. Structural analysis combined with site-directed mutagenesis defines the architecture of the active site.

PubMed: 14625590
DOI: 10.1038/nsb1017

実験手法

X-RAY DIFFRACTION (1.95 Å)