3ZD5

THE 2.2 A STRUCTURE OF A FULL-LENGTH CATALYTICALLY ACTIVE HAMMERHEAD RIBOZYME

「2GOZ」から置き換えられました

3ZD5 の概要

• エントリーDOI: 10.2210/pdb3zd5/pdb
• 関連するPDBエントリー: 3ZD4 3ZP8
• 分子名称: HAMMERHEAD RIBOZYME, ENZYME STRAND, HAMMERHEAD RIBOZYME, SUBSTRATE STRAND (3 entities in total)
• 機能のキーワード: catalytic rna, in-line attack, hammerhead rna, stem-loop interaction, uridine turn, a-form helix, rna
• 由来する生物種: Schistosoma mansoni; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20432.93

構造登録者

Martick, M.,Scott, W.G. (登録日: 2012-11-24, 公開日: 2012-12-12, 最終更新日: 2024-05-08)

主引用文献

Martick, M.,Scott, W.G.
Tertiary contacts distant from the active site prime a ribozyme for catalysis.
Cell, 126:309-320, 2006

PubMed Abstract: Minimal hammerhead ribozymes have been characterized extensively by static and time-resolved crystallography as well as numerous biochemical analyses, leading to mutually contradictory mechanistic explanations for catalysis. We present the 2.2 A resolution crystal structure of a full-length Schistosoma mansoni hammerhead ribozyme that permits us to explain the structural basis for its 1000-fold catalytic enhancement. The full-length hammerhead structure reveals how tertiary interactions occurring remotely from the active site prime this ribozyme for catalysis. G-12 and G-8 are positioned consistent with their previously suggested roles in acid-base catalysis, the nucleophile is aligned with a scissile phosphate positioned proximal to the A-9 phosphate, and previously unexplained roles of other conserved nucleotides become apparent within the context of a distinctly new fold that nonetheless accommodates the previous structural studies. These interactions permit us to explain the previously irreconcilable sets of experimental results in a unified, consistent, and unambiguous manner.

PubMed: 16859740
DOI: 10.1016/j.cell.2006.06.036

実験手法

X-RAY DIFFRACTION (2.2 Å)