3DHS

Mapping metal-binding sites in the catalytic domain of bacterial RNase P RNA

3DHS の概要

• エントリーDOI: 10.2210/pdb3dhs/pdb
• 関連するPDBエントリー: 2a64
• 分子名称: RNase P RNA, OSMIUM ION (2 entities in total)
• 機能のキーワード: catalytic rna, rna processing, hydrolase, rna
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 89857.16

構造登録者

Pace, N.R.,Kazantsev, A.V.,Krivenko, A.A. (登録日: 2008-06-18, 公開日: 2009-01-27, 最終更新日: 2023-08-30)

主引用文献

Kazantsev, A.V.,Krivenko, A.A.,Pace, N.R.
Mapping metal-binding sites in the catalytic domain of bacterial RNase P RNA
Rna, 15:266-276, 2009

PubMed Abstract: Ribonuclease P (RNase P) is a ribonucleoprotein enzyme that contains a universally conserved, catalytically active RNA component. RNase P RNA requires divalent metal ions for folding, substrate binding, and catalysis. Despite recent advances in understanding the structure of RNase P RNA, no comprehensive analysis of metal-binding sites has been reported, in part due to the poor crystallization properties of this large RNA. We have developed an abbreviated yet still catalytic construct, Bst P7Delta RNA, which contains the catalytic domain of the bacterial RNase P RNA and has improved crystallization properties. We use this mutant RNA as well as the native RNA to map metal-binding sites in the catalytic core of the bacterial RNase P RNA, by anomalous scattering in diffraction analysis. The results provide insight into the interplay between RNA structure and focalization of metal ions, and a structural basis for some previous biochemical observations with RNase P. We use electrostatic calculations to extract the potential functional significance of these metal-binding sites with respect to binding Mg(2+). The results suggest that with at least one important exception of specific binding, these sites mainly map areas of diffuse association of magnesium ions.

PubMed: 19095619
DOI: 10.1261/rna.1331809

実験手法

X-RAY DIFFRACTION (3.6 Å)