1PVO

X-ray crystal structure of Rho transcription termination factor in complex with ssRNA substrate and ANPPNP

1PVO の概要

• エントリーDOI: 10.2210/pdb1pvo/pdb
• 関連するPDBエントリー: 1PV4
• 分子名称: 5'-R(P*UP*C)-3', Transcription termination factor rho, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: rho-anppnp-ssrna complex, transcription-rna complex, transcription/rna
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 288290.13

構造登録者

Skordalakes, E.,Berger, J.M. (登録日: 2003-06-27, 公開日: 2003-07-22, 最終更新日: 2023-08-16)

主引用文献

Skordalakes, E.,Berger, J.M.
Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading
Cell(Cambridge,Mass.), 114:135-146, 2003

PubMed Abstract: In bacteria, one of the major transcriptional termination mechanisms requires a RNA/DNA helicase known as the Rho factor. We have determined two structures of Rho complexed with nucleic acid recognition site mimics in both free and nucleotide bound states to 3.0 A resolution. Both structures show that Rho forms a hexameric ring in which two RNA binding sites--a primary one responsible for target mRNA recognition and a secondary one required for mRNA translocation and unwinding--point toward the center of the ring. Rather than forming a closed ring, the Rho hexamer is split open, resembling a "lock washer" in its global architecture. The distance between subunits at the opening is sufficiently wide (12 A) to accommodate single-stranded RNA. This open configuration most likely resembles a state poised to load onto mRNA and suggests how related ring-shaped enzymes may be breached to bind nucleic acids.

PubMed: 12859904
DOI: 10.1016/S0092-8674(03)00512-9

実験手法

X-RAY DIFFRACTION (3 Å)