1M5K

Crystal structure of a hairpin ribozyme in the catalytically-active conformation

「1HP6」から置き換えられました

1M5K の概要

• エントリーDOI: 10.2210/pdb1m5k/pdb
• 関連するPDBエントリー: 1M5K 1M5O 1M5P 1M5V
• 分子名称: RNA INHIBITOR SUBSTRATE, RNA HAIRPIN RIBOZYME, PROTEIN (U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A), ... (6 entities in total)
• 機能のキーワード: hairpin ribozyme, catalytic rna, u1a rna binding protein docked conformation, substrate inhibitor strand, translation-rna complex, translation/rna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P09012
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 97809.71

構造登録者

Rupert, P.B.,Ferre-D'Amare, A.R. (登録日: 2002-07-09, 公開日: 2002-08-02, 最終更新日: 2024-02-14)

主引用文献

Rupert, P.B.,Massey, A.P.,Sigurdsson, S.T.,Ferre-D'Amare, A.R.
Transition state stabilization by a catalytic RNA
Science, 298:1421-1424, 2002

PubMed Abstract: The hairpin ribozyme catalyses sequence-specific cleavage of RNA. The active site of this natural RNA results from the docking of two irregular helices: stems A and B. One strand of stem A harbours the scissile bond. The 2.4 A resolution structure of a hairpin ribozyme-inhibitor complex reveals that the ribozyme aligns the 2'-OH nucleophile and the 5'-oxo leaving group by twisting apart the nucleotides that flank the scissile phosphate. The base of the nucleotide preceding the cleavage site is stacked within stem A; the next nucleotide, a conserved guanine, is extruded from stem A and accommodated by a highly complementary pocket in the minor groove of stem B. Metal ions are absent from the active site. The bases of four conserved purines are positioned potentially to serve as acid-base catalysts. This is the first structure determination of a fully assembled ribozyme active site that catalyses a phosphodiester cleavage without recourse to metal ions.

PubMed: 11298439
DOI: 10.1126/science.1076093

実験手法

X-RAY DIFFRACTION (2.4 Å)