1NBS

Crystal structure of the specificity domain of Ribonuclease P RNA

1NBS の概要

• エントリーDOI: 10.2210/pdb1nbs/pdb
• 関連するPDBエントリー: 1NXL
• 分子名称: RIBONUCLEASE P RNA, MAGNESIUM ION, LEAD (II) ION (3 entities in total)
• 機能のキーワード: ribonuclease p rna, p rna, s-domain, rna
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 105477.15

構造登録者

Krasilnikov, A.S.,Yang, X.,Pan, T.,Mondragon, A. (登録日: 2002-12-03, 公開日: 2003-02-18, 最終更新日: 2024-02-14)

主引用文献

Krasilnikov, A.S.,Yang, X.,Pan, T.,Mondragon, A.
Crystal structure of the specificity domain of Ribonuclease P
Nature, 421:760-764, 2003

PubMed Abstract: RNase P is the only endonuclease responsible for processing the 5' end of transfer RNA by cleaving a precursor and leading to tRNA maturation. It contains an RNA component and a protein component and has been identified in all organisms. It was one of the first catalytic RNAs identified and the first that acts as a multiple-turnover enzyme in vivo. RNase P and the ribosome are so far the only two ribozymes known to be conserved in all kingdoms of life. The RNA component of bacterial RNase P can catalyse pre-tRNA cleavage in the absence of the RNase P protein in vitro and consists of two domains: a specificity domain and a catalytic domain. Here we report a 3.15-A resolution crystal structure of the 154-nucleotide specificity domain of Bacillus subtilis RNase P. The structure reveals the architecture of this domain, the interactions that maintain the overall fold of the molecule, a large non-helical but well-structured module that is conserved in all RNase P RNA, and the regions that are involved in interactions with the substrate.

PubMed: 12610630
DOI: 10.1038/nature01386

実験手法

X-RAY DIFFRACTION (3.15 Å)