2HT1

The closed ring structure of the Rho transcription termination factor in complex with nucleic acid in the motor domains

2HT1 の概要

• エントリーDOI: 10.2210/pdb2ht1/pdb
• 関連するPDBエントリー: 1PV4 1PVO
• 分子名称: 5'-R(*UP*C)-3', 5'-R(*UP*CP*UP*CP*U)-3', Transcription termination factor rho, ... (4 entities in total)
• 機能のキーワード: atpase, translocase, hydrolase-rna complex, hydrolase/rna
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 99797.75

構造登録者

Skordalakes, E.,Berger, J.M. (登録日: 2006-07-24, 公開日: 2006-11-14, 最終更新日: 2023-08-30)

主引用文献

Skordalakes, E.,Berger, J.M.
Structural Insights into RNA-Dependent Ring Closure and ATPase Activation by the Rho Termination Factor.
Cell(Cambridge,Mass.), 127:553-564, 2006

PubMed Abstract: Hexameric helicases and translocases are required for numerous essential nucleic-acid transactions. To better understand the mechanisms by which these enzymes recognize target substrates and use nucleotide hydrolysis to power molecular movement, we have determined the structure of the Rho transcription termination factor, a hexameric RNA/DNA helicase, with single-stranded RNA bound to the motor domains of the protein. The structure reveals a closed-ring "trimer of dimers" conformation for the hexamer that contains an unanticipated arrangement of conserved loops required for nucleic-acid translocation. RNA extends across a shallow intersubunit channel formed by conserved amino acids required for RNA-stimulated ATP hydrolysis and translocation and directly contacts a conserved lysine, just upstream of the catalytic GKT triad, in the phosphate-binding (P loop) motif of the ATP-binding pocket. The structure explains the molecular effects of numerous mutations and provides new insights into the links between substrate recognition, ATP turnover, and coordinated strand movement.

PubMed: 17081977
DOI: 10.1016/j.cell.2006.08.051

実験手法

X-RAY DIFFRACTION (3.51 Å)